S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC 2.3.1.26.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
An enzyme that catalyses the last step of the TRIACYLGLYCEROL synthesis reaction in which diacylglycerol is covalently joined to LONG-CHAIN ACYL COA to form triglyceride. It was formerly categorized as EC 2.3.1.124.
An enzyme that catalyzes the acyl group transfer of acyl COENZYME A to RETINOL to generate COENZYME A and a retinyl ester.
A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
An 86-amino acid polypeptide, found in central and peripheral tissues, that displaces diazepam from the benzodiazepine recognition site on the gamma-aminobutyric acid receptor (RECEPTORS, GABA). It also binds medium- and long-chain acyl-CoA esters and serves as an acyl-CoA transporter. This peptide regulates lipid metabolism.
An enzyme that catalyzes the first and rate-determining steps of peroxisomal beta-oxidation of fatty acids. It acts on COENZYME A derivatives of fatty acids with chain lengths from 8 to 18, using FLAVIN-ADENINE DINUCLEOTIDE as a cofactor.
Organic compounds that contain silicon as an integral part of the molecule.
A plastic substance deposited by insects or obtained from plants. Waxes are esters of various fatty acids with higher, usually monohydric alcohols. The wax of pharmacy is principally yellow wax (beeswax), the material of which honeycomb is made. It consists chiefly of cerotic acid and myricin and is used in making ointments, cerates, etc. (Dorland, 27th ed)
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
Eighteen carbon fatty acids that comprise the great majority of CASTOR OIL, which is from the seed of RICINUS.
A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.
A family of gram-positive bacteria found in soil and dairy products and as parasites on animals and man. Several are important pathogens.
Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.
Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.
An autosomal recessive disorder of fatty acid oxidation, and branched chain amino acids (AMINO ACIDS, BRANCHED-CHAIN); LYSINE; and CHOLINE catabolism, that is due to defects in either subunit of ELECTRON TRANSFER FLAVOPROTEIN or its dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase (EC 1.5.5.1).
A family of enzymes that catalyze the stereoselective, regioselective, or chemoselective syn-dehydrogenation reactions. They function by a mechanism that is linked directly to reduction of molecular OXYGEN.
Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.
The rate dynamics in chemical or physical systems.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.
Compounds with three contiguous nitrogen atoms in linear format, H2N-N=NH, and hydrocarbyl derivatives.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
A class of organic compounds containing a ring structure made up of more than one kind of atom, usually carbon plus another atom. The ring structure can be aromatic or nonaromatic.
Fatty acid esters of cholesterol which constitute about two-thirds of the cholesterol in the plasma. The accumulation of cholesterol esters in the arterial intima is a characteristic feature of atherosclerosis.
An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.
A mitosporic fungal species used in the production of penicillin.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Derivatives of caprylic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated eight carbon aliphatic structure.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.
"Esters are organic compounds that result from the reaction between an alcohol and a carboxylic acid, playing significant roles in various biological processes and often used in pharmaceutical synthesis."
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. Enzymes in this group are instrumental in ketone body metabolism and utilization of acetoacetate in mitochondria. EC 2.8.3.
The process of converting an acid into an alkyl or aryl derivative. Most frequently the process consists of the reaction of an acid with an alcohol in the presence of a trace of mineral acid as catalyst or the reaction of an acyl chloride with an alcohol. Esterification can also be accomplished by enzymatic processes.
Cobamides are a class of compounds that function as cofactors in various enzymatic reactions, containing a corrin ring similar to vitamin B12, but with different substituents on the benzimidazole moiety, and can be found in certain bacteria and archaea.
A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A sulfhydryl compound used to prevent urothelial toxicity by inactivating metabolites from ANTINEOPLASTIC AGENTS, such as IFOSFAMIDE or CYCLOPHOSPHAMIDE.
An unsaturated fatty acid that is the most widely distributed and abundant fatty acid in nature. It is used commercially in the preparation of oleates and lotions, and as a pharmaceutical solvent. (Stedman, 26th ed)
The addition of an organic acid radical into a molecule.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
A butyryl-beta-alanine that can also be viewed as pantoic acid complexed with BETA ALANINE. It is incorporated into COENZYME A and protects cells against peroxidative damage by increasing the level of GLUTATHIONE.
Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.
An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.
Proteins found in any species of bacterium.
Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
The functional hereditary units of BACTERIA.
The sum of the weight of all the atoms in a molecule.
Triglycerides are the most common type of fat in the body, stored in fat cells and used as energy; they are measured in blood tests to assess heart disease risk, with high levels often resulting from dietary habits, obesity, physical inactivity, smoking, and alcohol consumption.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A phylum of ARCHAEA comprising at least seven classes: Methanobacteria, Methanococci, Halobacteria (extreme halophiles), Archaeoglobi (sulfate-reducing species), Methanopyri, and the thermophiles: Thermoplasmata, and Thermococci.
An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.
A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
Mevalonic acid is a crucial intermediate compound in the HMG-CoA reductase pathway, which is a metabolic route that produces cholesterol, other steroids, and isoprenoids in cells.
Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.
Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.
A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.
A fungal metabolite isolated from cultures of Aspergillus terreus. The compound is a potent anticholesteremic agent. It inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It also stimulates the production of low-density lipoprotein receptors in the liver.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a choline moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and choline and 2 moles of fatty acids.
The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.
An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
The simplest saturated hydrocarbon. It is a colorless, flammable gas, slightly soluble in water. It is one of the chief constituents of natural gas and is formed in the decomposition of organic matter. (Grant & Hackh's Chemical Dictionary, 5th ed)
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Oxidoreductases that are specific for ALDEHYDES.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
The characteristic three-dimensional shape of a molecule.
Cyclic TETRAPYRROLES based on the corrin skeleton.
A derivative of LOVASTATIN and potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It may also interfere with steroid hormone production. Due to the induction of hepatic LDL RECEPTORS, it increases breakdown of LDL CHOLESTEROL.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
A cobalt-containing coordination compound produced by intestinal micro-organisms and found also in soil and water. Higher plants do not concentrate vitamin B 12 from the soil and so are a poor source of the substance as compared with animal tissues. INTRINSIC FACTOR is important for the assimilation of vitamin B 12.
An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.
Steroids with a hydroxyl group at C-3 and most of the skeleton of cholestane. Additional carbon atoms may be present in the side chain. (IUPAC Steroid Nomenclature, 1987)
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
Thiolester hydrolases are enzymes that catalyze the hydrolysis of thioester bonds, commonly found in acetyl-CoA and other coenzyme A derivatives, to produce free carboxylic acids and CoASH.
Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.
This enzyme catalyzes the transacylation of malonate from MALONYL CoA to activated holo-ACP, to generate malonyl-(acyl-carrier protein), which is an elongation substrate in FATTY ACIDS biosynthesis. It is an essential enzyme in the biosynthesis of FATTY ACIDS in all BACTERIA.
**Mercaptoethanol, also known as β-mercaptoethanol or BME, is an organosulfur compound with the formula HOCH2CH2SH, functionally serving as a reducing agent and a sulfhydryl group protector in biochemical and molecular biology applications.**
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.
An enzyme that catalyzes the synthesis of hydroxymethylglutaryl-CoA from acetyl-CoA and acetoacetyl-CoA. This is a key enzyme in steroid biosynthesis. This enzyme was formerly listed as EC 4.1.3.5.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to an ethanolamine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and ethanolamine and 2 moles of fatty acids.
A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.
An enzyme of long-chain fatty acid synthesis, that adds a two-carbon unit from malonyl-(acyl carrier protein) to another molecule of fatty acyl-(acyl carrier protein), giving a beta-ketoacyl-(acyl carrier protein) with the release of carbon dioxide. EC 2.3.1.41.
An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.
The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.
Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A group of 16-carbon fatty acids that contain no double bonds.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Glutarates are organic compounds, specifically carboxylic acids, that contain a five-carbon chain with two terminal carboxyl groups and a central methyl group, playing a role in various metabolic processes, including the breakdown of certain amino acids. They can also refer to their salts or esters. Please note that this definition is concise and may not cover all aspects of glutarates in depth.
Proteins prepared by recombinant DNA technology.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)
Differential thermal analysis in which the sample compartment of the apparatus is a differential calorimeter, allowing an exact measure of the heat of transition independent of the specific heat, thermal conductivity, and other variables of the sample.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
Enzymes that catalyze the first step leading to the oxidation of succinic acid by the reversible formation of succinyl-CoA from succinate and CoA with the concomitant cleavage of ATP to ADP (EC 6.2.1.5) or GTP to GDP (EC 6.2.1.4) and orthophosphate. Itaconate can act instead of succinate and ITP instead of GTP.EC 6.2.1.-.
Malonates are organic compounds containing a malonate group, which is a dicarboxylic acid functional group with the structure -OC(CH2COOH)2, and can form salts or esters known as malonates.
FATTY ACIDS in which the carbon chain contains one or more double or triple carbon-carbon bonds.
An enzyme that catalyzes the formation of acetoacetyl-CoA from two molecules of ACETYL COA. Some enzymes called thiolase or thiolase-I have referred to this activity or to the activity of ACETYL-COA C-ACYLTRANSFERASE.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.
A genus of gram-negative, aerobic, rod-shaped bacteria found in wet soil containing decaying organic material and in water. Cells tend to be pleomorphic if grown on media containing succinate or coccoid if grown in the presence of an alcohol as the sole carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.
A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.
7-carbon saturated monocarboxylic acids.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and the CoA ester of a fatty acid two carbons shorter is formed.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.
Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.
Compounds containing the -SH radical.
Biological catalysts and their cofactors.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.
Methyl, propyl, butyl, and ethyl esters of p-hydroxybenzoic acid. They have been approved by the FDA as antimicrobial agents for foods and pharmaceuticals. (From Hawley's Condensed Chemical Dictionary, 11th ed, p872)
A colorless, flammable liquid used in the manufacture of FORMALDEHYDE and ACETIC ACID, in chemical synthesis, antifreeze, and as a solvent. Ingestion of methanol is toxic and may cause blindness.
Any salt or ester of glycerophosphoric acid.
Dimethylamines are organic compounds that contain two methyl groups (-CH3) bonded to a nitrogen atom (N), with the general formula (CH3)2NH. They can act as secondary amines and are commonly used in chemical synthesis, but they are not typically found as natural components in the human body.
Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.
Compounds based on 2-amino-4-hydroxypteridine.
A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.
Measurement of the intensity and quality of fluorescence.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Proteins found in any species of archaeon.
A class of sphingolipids found largely in the brain and other nervous tissue. They contain phosphocholine or phosphoethanolamine as their polar head group so therefore are the only sphingolipids classified as PHOSPHOLIPIDS.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
An important intermediate in lipid biosynthesis and in glycolysis.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.

Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. (1/1356)

In nonribosomal biosynthesis of peptide antibiotics by multimodular synthetases, amino acid monomers are activated by the adenylation domains of the synthetase and loaded onto the adjacent carrier protein domains as thioesters, then the formation of peptide bonds and translocation of the growing chain are effected by the synthetase's condensation domains. Whether the condensation domains have any editing function has been unknown. Synthesis of aminoacyl-coenzyme A (CoA) molecules and direct enzymatic transfer of aminoacyl-phosphopantetheine to the carrier domains allow the adenylation domain editing function to be bypassed. This method was used to demonstrate that the first condensation domain of tyrocidine synthetase shows low selectivity at the donor residue (D-phenylalanine) and higher selectivity at the acceptor residue (L-proline) in the formation of the chain-initiating D-Phe-L-Pro dipeptidyl-enzyme intermediate.  (+info)

Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. (2/1356)

The activities of beta-oxidation enzymes were measured in extracts of glucose- and triolein-grown cells of Aspergillus niger. Growth on triolein stimulated increased enzyme activity, especially for acyl-CoA dehydrogenase. No acyl-CoA oxidase activity was detected. HPLC analysis after incubation of triolein-grown cell extracts with decanoyl-CoA showed that beta-oxidation was limited to one cycle. Octanoyl-CoA accumulated as the decanoyl-CoA was oxidized. Beta-oxidation enzymes in isolated mitochondrial fractions were also studied. The results are discussed in the context of methyl ketone production by fungi.  (+info)

Inositol acylation of glycosylphosphatidylinositols in the pathogenic fungus Cryptococcus neoformans and the model yeast Saccharomyces cerevisiae. (3/1356)

Cryptococcus neoformans, an opportunistic fungus responsible for life-threatening infection in immunocompromised patients, is able to synthesize glycosylphosphatidylinositol (GPI) structures. Radiolabelling experiments in vitro with the use of a cryptococcal cell-free system showed that the pathway begins as in other eukaryotes, with the addition of N-acetylglucosamine to phosphatidylinositol, followed by deacetylation of the sugar residue. The third step, acylation of the inositol ring, seemed to involve a fatty acid other than palmitate, in contrast with previous findings in Saccharomyces cerevisiae and mammalian GPI pathways. A systematic study of inositol acylation in C. neoformans and S. cerevisiae showed that both organisms used a variety of fatty acids in this step; these were transferred directly from acyl-CoA to inositol without modification. However, the specificity of fatty acid utilization was quite distinct in the two fungi, with the pathogen being substantially more restrictive. In mammalian cells fatty acids added exogenously as acyl-CoAs are not transferred directly to inositol. These results suggest significant differences in the GPI biosynthetic pathway between mammalian and C. neoformans cells that could represent targets for anti-cryptococcal therapy.  (+info)

Delta3,5,7,Delta2,4,6-trienoyl-CoA isomerase, a novel enzyme that functions in the beta-oxidation of polyunsaturated fatty acids with conjugated double bonds. (4/1356)

The mitochondrial metabolism of unsaturated fatty acids with conjugated double bonds at odd-numbered positions, e.g. 9-cis, 11-trans-octadecadienoic acid, was investigated. These fatty acids are substrates of beta-oxidation in isolated rat liver mitochondria and hence are expected to yield 5,7-dienoyl-CoA intermediates. 5, 7-Decadienoyl-CoA was used to study the degradation of these intermediates. After introduction of a 2-trans-double bond by acyl-CoA dehydrogenase or acyl-CoA oxidase, the resultant 2,5, 7-decatrienoyl-CoA can either continue its pass through the beta-oxidation cycle or be converted by Delta3,Delta2-enoyl-CoA isomerase to 3,5,7-decatrienoyl-CoA. The latter compound was isomerized by a novel enzyme, named Delta3,5,7,Delta2,4, 6-trienoyl-CoA isomerase, to 2,4,6-decatrienoyl-CoA, which is a substrate of 2,4-dienoyl-CoA reductase (Wang, H.-Y. and Schulz, H. (1989) Biochem. J. 264, 47-52) and hence can be completely degraded via beta-oxidation. Delta3,5,7,Delta2,4,6-Trienoyl-CoA isomerase was purified from pig heart to apparent homogeneity and found to be a component enzyme of Delta3,5,Delta2,4-dienoyl-CoA isomerase. Although the direct beta-oxidation of 2,5,7-decatrienoyl-CoA seems to be the major pathway, the degradation via 2,4,6-trienoyl-CoA makes a significant contribution to the total beta-oxidation of this intermediate.  (+info)

Carbon-13 nuclear magnetic resonance study of metabolism of propionate by Escherichia coli. (5/1356)

We have evaluated the use of [1,2-13C2]propionate for the analysis of propionic acid metabolism, based on the ability to distinguish between the methylcitrate and methylmalonate pathways. Studies using propionate-adapted Escherichia coli MG1655 cells were performed. Preservation of the 13C-13C-12C carbon skeleton in labeled alanine and alanine-containing peptides involved in cell wall recycling is indicative of the direct formation of pyruvate from propionate via the methylcitrate cycle, the enzymes of which have recently been demonstrated in E. coli. Additionally, formation of 13C-labeled formate from pyruvate by the action of pyruvate-formate lyase is also consistent with the labeling of pyruvate C-1. Carboxylation of the labeled pyruvate leads to formation of [1,2-13C2]oxaloacetate and to multiply labeled glutamate and succinate isotopomers, also consistent with the flux through the methylcitrate pathway, followed by the tricarboxylic acid (TCA) cycle. Additional labeling of TCA intermediates arises due to the formation of [1-13C]acetyl coenzyme A from the labeled pyruvate, formed via pyruvate-formate lyase. Labeling patterns in trehalose and glycine are also interpreted in terms of the above pathways. The information derived from the [1, 2-13C2]propionate label is contrasted with information which can be derived from singly or triply labeled propionate and shown to be more useful for distinguishing the different propionate utilization pathways via nuclear magnetic resonance analysis.  (+info)

Purification, characterization, DNA sequence and cloning of a pimeloyl-CoA synthetase from Pseudomonas mendocina 35. (6/1356)

A pimeloyl-CoA synthetase from Pseudomonas mendocina 35 was purified and characterized, the DNA sequence determined, and the gene cloned into Escherichia coli to yield an active enzyme. The purified enzyme had a pH optimum of approximately 8.0, Km values of 0.49 mM for pimelic acid, 0.18 mM for CoA and 0.72 mM for ATP, a subunit Mr of approximately 80000 as determined by SDS/PAGE, and was found to be a tetramer by gel-filtration chromatography. The specific activity of the purified enzyme was 77.3 units/mg of protein. The enzyme was not absolutely specific for pimelic acid. The relative activity for adipic acid (C6) was 72% and for azaleic acid (C9) was 18% of that for pimelic acid (C7). The N-terminal amino acid was blocked to amino acid sequencing, but controlled proteolysis resulted in three peptide fragments for which amino acid sequences were obtained. An oligonucleotide gene probe corresponding to one of the amino acid sequences was synthesized and used to isolate the gene (pauA, pimelic acid-utilizing A) coding for pimeloyl-CoA synthetase. The pauA gene, which codes for a protein with a theoretical Mr of 74643, was then sequenced. The deduced amino acid sequence of the enzyme showed similarity to hypothetical proteins from Archaeoglobus fulgidus, Methanococcus jannaschii, Pyrococcus horikoshii, E. coli and Streptomyces coelicolor, and some limited similarity to microbial succinyl-CoA synthetases. The similarity with the protein from A. fulgidus was especially strong, thus indicating a function for this unidentified protein. The pauA gene was cloned into E. coli, where it was expressed and resulted in an active enzyme.  (+info)

Short-chain acyl-CoA-dependent production of oxalate from oxaloacetate by Burkholderia glumae, a plant pathogen which causes grain rot and seedling rot of rice via the oxalate production. (7/1356)

In Burkholderia glumae (formerly named Pseudomonas glumae), isolated as the causal agent of grain rot and seedling rot of rice, oxalate was produced from oxaloacetate in the presence of short-chain acyl-CoA such as acetyl-CoA and propionyl-CoA. Upon purification, the enzyme responsible was separated into two fractions (tentatively named fractions II and III), both of which were required for the acyl-CoA-dependent production of oxalate. In conjugation with the oxalate production from oxaloacetate catalyzed by fractions II and III, acetyl-CoA used as the acyl-CoA substrate was consumed and equivalent amounts of CoASH and acetoacetate were formed. The isotope incorporation pattern indicated that the two carbon atoms of oxalate are both derived from oxaloacetate, and among the four carbon atoms of acetoacetate two are from oxaloacetate and two from acetyl-CoA. When the reaction was carried out with fraction II alone, a decrease in acetyl-CoA and an equivalent level of net utilization of oxaloacetate were observed without appreciable formation of CoASH, acetoacetate or oxalate. It appears that in the oxalate production from oxaloacetate and acetyl-CoA, fraction II catalyzes condensation of the two substrates to form an intermediate which is split into oxalate and acetoacetate by fraction III being accompanied by the release of CoASH.  (+info)

NIH shift in flavin-dependent monooxygenation: mechanistic studies with 2-aminobenzoyl-CoA monooxygenase/reductase. (8/1356)

The flavoprotein 2-aminobenzoyl-CoA monooxygenase/reductase from the eubacterium Azoarcus evansii catalyzes the dearomatization of 2-aminobenzoyl-CoA. The reaction consists in an O2-dependent monooxygenation at the benzene position 5, which is followed immediately by an NADH-dependent hydrogenation of the intermediate at the same catalytic locus. The reaction was studied by 1H, 2H, and 13C NMR spectroscopy of the products. The main product was characterized as 5-oxo-2-aminocyclohex-1-ene-1-carboxyl-CoA by two-dimensional NMR spectroscopy. Thus, [5-2H]2-aminobenzoyl-CoA was converted into [6-2H]5-oxo-2-aminocyclohex-1-ene-1-carboxyl-CoA, indicating a 5 --> 6 shift of the [5-2H] label. Label from NAD2H was transferred to the 3 position of the cyclic eneamine, whereas label from solvent D2O was incorporated into the 4 and the 6 positions of 5-oxo-2-aminocyclohex-1-ene-1-carboxyl-CoA. The labeling pattern is compatible with the monooxygenation proceeding via what is formally an NIH shift, yielding 5-oxo-2-aminocyclohex-1, 3-diene-1-carboxyl-CoA as a protein-bound intermediate. It is suggested that this shift in flavin-dependent monooxygenation may have general validity.  (+info)

Acyl Coenzyme A (often abbreviated as Acetyl-CoA or Acyl-CoA) is a crucial molecule in metabolism, particularly in the breakdown and oxidation of fats and carbohydrates to produce energy. It is a thioester compound that consists of a fatty acid or an acetate group linked to coenzyme A through a sulfur atom.

Acyl CoA plays a central role in several metabolic pathways, including:

1. The citric acid cycle (Krebs cycle): In the mitochondria, Acyl-CoA is formed from the oxidation of fatty acids or the breakdown of certain amino acids. This Acyl-CoA then enters the citric acid cycle to produce high-energy electrons, which are used in the electron transport chain to generate ATP (adenosine triphosphate), the main energy currency of the cell.
2. Beta-oxidation: The breakdown of fatty acids occurs in the mitochondria through a process called beta-oxidation, where Acyl-CoA is sequentially broken down into smaller units, releasing acetyl-CoA, which then enters the citric acid cycle.
3. Ketogenesis: In times of low carbohydrate availability or during prolonged fasting, the liver can produce ketone bodies from acetyl-CoA to supply energy to other organs, such as the brain and heart.
4. Protein synthesis: Acyl-CoA is also involved in the modification of proteins by attaching fatty acid chains to them (a process called acetylation), which can influence protein function and stability.

In summary, Acyl Coenzyme A is a vital molecule in metabolism that connects various pathways related to energy production, fatty acid breakdown, and protein modification.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

Coenzyme A (CoA) ligases, also known as CoA synthetases, are a class of enzymes that activate acyl groups, such as fatty acids and amino acids, by forming a thioester bond with coenzyme A. This activation is an essential step in various metabolic pathways, including fatty acid oxidation, amino acid catabolism, and the synthesis of several important compounds like steroids and acetylcholine.

CoA ligases catalyze the following reaction:

acyl group + ATP + CoA ↔ acyl-CoA + AMP + PP~i~

In this reaction, an acyl group (R-) from a carboxylic acid is linked to the thiol (-SH) group of coenzyme A through a high-energy thioester bond. The energy required for this activation is provided by the hydrolysis of ATP to AMP and inorganic pyrophosphate (PP~i~).

CoA ligases are classified into three main types based on the nature of the acyl group they activate:

1. Acyl-CoA synthetases (or long-chain fatty acid CoA ligases) activate long-chain fatty acids, typically containing 12 or more carbon atoms.
2. Aminoacyl-CoA synthetases activate amino acids to form aminoacyl-CoAs, which are essential intermediates in the catabolism of certain amino acids.
3. Short-chain specific CoA ligases activate short-chain fatty acids (up to 6 carbon atoms) and other acyl groups like acetate or propionate.

These enzymes play a crucial role in maintaining cellular energy homeostasis, metabolism, and the synthesis of various essential biomolecules.

Sterol O-Acyltransferase (SOAT, also known as ACAT for Acyl-CoA:cholesterol acyltransferase) is an enzyme that plays a crucial role in cholesterol homeostasis within cells. Specifically, it catalyzes the reaction of esterifying free cholesterol with fatty acyl-coenzyme A (fatty acyl-CoA) to form cholesteryl esters. This enzymatic activity allows for the intracellular storage of excess cholesterol in lipid droplets, reducing the levels of free cholesterol in the cell and thus preventing its potential toxic effects on membranes and proteins. There are two isoforms of SOAT, SOAT1 and SOAT2, which exhibit distinct subcellular localization and functions. Dysregulation of SOAT activity has been implicated in various pathological conditions, including atherosclerosis and neurodegenerative disorders.

Coenzymes are small organic molecules that assist enzymes in catalyzing chemical reactions within cells. They typically act as carriers of specific atoms or groups of atoms during enzymatic reactions, facilitating the conversion of substrates into products. Coenzymes often bind temporarily to enzymes at the active site, forming an enzyme-coenzyme complex.

Coenzymes are usually derived from vitamins or minerals and are essential for maintaining proper metabolic functions in the body. Examples of coenzymes include nicotinamide adenine dinucleotide (NAD+), flavin adenine dinucleotide (FAD), and coenzyme A (CoA). When a coenzyme is used up in a reaction, it must be regenerated or replaced for the enzyme to continue functioning.

In summary, coenzymes are vital organic compounds that work closely with enzymes to facilitate biochemical reactions, ensuring the smooth operation of various metabolic processes within living organisms.

Acyltransferases are a group of enzymes that catalyze the transfer of an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydrogen atom) from one molecule to another. This transfer involves the formation of an ester bond between the acyl group donor and the acyl group acceptor.

Acyltransferases play important roles in various biological processes, including the biosynthesis of lipids, fatty acids, and other metabolites. They are also involved in the detoxification of xenobiotics (foreign substances) by catalyzing the addition of an acyl group to these compounds, making them more water-soluble and easier to excrete from the body.

Examples of acyltransferases include serine palmitoyltransferase, which is involved in the biosynthesis of sphingolipids, and cholesteryl ester transfer protein (CETP), which facilitates the transfer of cholesteryl esters between lipoproteins.

Acyltransferases are classified based on the type of acyl group they transfer and the nature of the acyl group donor and acceptor molecules. They can be further categorized into subclasses based on their sequence similarities, three-dimensional structures, and evolutionary relationships.

Diacylglycerol O-Acyltransferase (DGAT) is an enzyme that catalyzes the final step in triacylglycerol synthesis, which is the formation of diacylglycerol and fatty acyl-CoA into triacylglycerol. This enzyme plays a crucial role in lipid metabolism and energy storage in cells. There are two main types of DGAT enzymes, DGAT1 and DGAT2, which share limited sequence similarity but have similar functions. Inhibition of DGAT has been explored as a potential therapeutic strategy for the treatment of obesity and related metabolic disorders.

Retinol O-fatty-acyltransferase is not a widely recognized or established term in medical literature. However, I can provide information on the related concepts that might help you understand the term.

The enzyme likely being referred to here is lecithin-retinol acyltransferase (LRAT), which is involved in the visual cycle and is responsible for the esterification of retinol (vitamin A alcohol) into retinyl esters. This reaction occurs in the eye's pigment epithelium, where LRAT adds a fatty acid to retinol, forming retinyl palmitate, which is then stored in the retinal pigment epithelium (RPE).

The term "Retinol O-fatty-acyltransferase" seems to be an attempt to describe LRAT's function more generally. However, it is not a standard or widely accepted term for this enzyme in medical and scientific literature.

Palmitoyl Coenzyme A, often abbreviated as Palmitoyl-CoA, is a type of fatty acyl coenzyme A that plays a crucial role in the body's metabolism. It is formed from the esterification of palmitic acid (a saturated fatty acid) with coenzyme A.

Medical Definition: Palmitoyl Coenzyme A is a fatty acyl coenzyme A ester, where palmitic acid is linked to coenzyme A via an ester bond. It serves as an important intermediate in lipid metabolism and energy production, particularly through the process of beta-oxidation in the mitochondria. Palmitoyl CoA also plays a role in protein modification, known as S-palmitoylation, which can affect protein localization, stability, and function.

Acyl-CoA dehydrogenase is a group of enzymes that play a crucial role in the body's energy production process. Specifically, they are involved in the breakdown of fatty acids within the cells.

More technically, acyl-CoA dehydrogenases catalyze the removal of electrons from the thiol group of acyl-CoAs, forming a trans-double bond and generating FADH2. This reaction is the first step in each cycle of fatty acid beta-oxidation, which occurs in the mitochondria of cells.

There are several different types of acyl-CoA dehydrogenases, each specific to breaking down different lengths of fatty acids. For example, very long-chain acyl-CoA dehydrogenase (VLCAD) is responsible for breaking down longer chain fatty acids, while medium-chain acyl-CoA dehydrogenase (MCAD) breaks down medium-length chains.

Deficiencies in these enzymes can lead to various metabolic disorders, such as MCAD deficiency or LC-FAOD (long-chain fatty acid oxidation disorders), which can cause symptoms like vomiting, lethargy, and muscle weakness, especially during periods of fasting or illness.

A Diazepam Binding Inhibitor (DBI) is a protein that inhibits the binding of benzodiazepines, such as diazepam, to their receptor site in the central nervous system. DBI is also known as the alpha-2-macroglobulin-like protein 1 or A2ML1. It is involved in regulating the activity of the GABA-A receptor complex, which plays a crucial role in inhibitory neurotransmission in the brain. When DBI binds to the benzodiazepine site on the GABA-A receptor, it prevents diazepam and other benzodiazepines from exerting their effects, which include sedation, anxiety reduction, muscle relaxation, and anticonvulsant activity.

Acyl-CoA oxidase is an enzyme that plays a crucial role in the breakdown of fatty acids within the body. It is located in the peroxisomes, which are small organelles found in the cells of living organisms. The primary function of acyl-CoA oxidase is to catalyze the initial step in the beta-oxidation of fatty acids, a process that involves the sequential removal of two-carbon units from fatty acid molecules in the form of acetyl-CoA.

The reaction catalyzed by acyl-CoA oxidase is as follows:

acyl-CoA + FAD → trans-2,3-dehydroacyl-CoA + FADH2 + H+

In this reaction, the enzyme removes a hydrogen atom from the fatty acyl-CoA molecule and transfers it to its cofactor, flavin adenine dinucleotide (FAD). This results in the formation of trans-2,3-dehydroacyl-CoA, FADH2, and a proton. The FADH2 produced during this reaction can then be used to generate ATP through the electron transport chain, while the trans-2,3-dehydroacyl-CoA undergoes further reactions in the beta-oxidation pathway.

There are two main isoforms of acyl-CoA oxidase found in humans: ACOX1 and ACOX2. ACOX1 is primarily responsible for oxidizing straight-chain fatty acids, while ACOX2 specializes in the breakdown of branched-chain fatty acids. Mutations in the genes encoding these enzymes can lead to various metabolic disorders, such as peroxisomal biogenesis disorders and Refsum disease.

Organosilicon compounds are a class of chemical compounds that contain at least one organic group (a group of atoms composed mainly of carbon and hydrogen) bonded to a silicon atom. The organic group can be an alkyl group, aryl group, or any other group that is derived from a hydrocarbon.

The term "organosilicon" is used to describe the covalent bond between carbon and silicon atoms, which is a type of bond known as a "sigma bond." This bond is formed by the overlap of atomic orbitals between the carbon and silicon atoms. The resulting organosilicon compound can have a wide range of physical and chemical properties, depending on the nature of the organic group and the number of such groups attached to the silicon atom.

Organosilicon compounds are widely used in various industries, including electronics, coatings, adhesives, and pharmaceuticals. They are also used as intermediates in the synthesis of other chemical compounds. Some common examples of organosilicon compounds include silicones, which are polymers that contain repeating units of siloxane (Si-O-Si) bonds, and organofunctional silanes, which are used as coupling agents to improve the adhesion of materials to surfaces.

I believe you may be asking for a medical explanation or examples of substances that are referred to as "waxes." Waxes are not a specific medical term, but they can refer to various natural or synthetic esters that are insoluble in water and have a soft, waxy consistency. In a medical context, the term "waxes" might refer to:

1. Cerumen (Earwax): A yellowish waxy substance produced by glands in the ear canal. Cerumen helps protect the ear by trapping dirt, dust, and other particles and preventing them from entering the inner ear.
2. Sebaceous Waxes: These are esters found in sebum, an oily substance produced by sebaceous glands in the skin. Sebum helps keep the skin and hair moisturized and protected.
3. Cutaneous Waxes: These are lipid-rich substances secreted by specialized sweat glands called eccrine glands. They help to waterproof and protect the skin.
4. Histological Waxes: Paraffin or other waxes used in histology for tissue processing, embedding, and microtomy to prepare thin sections of tissues for examination under a microscope.

These are some examples of substances that can be referred to as "waxes" in a medical context.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Ricinoleic acid is not typically defined in the context of medical terminology, but it is a chemical compound with potential medical relevance. It is a fatty acid that is the main constituent of castor oil, which is obtained from the seeds of the Ricinus communis plant. Ricinoleic acid has been studied for its potential medicinal properties, including its anti-inflammatory, analgesic, and antibacterial effects. However, it is important to note that ricinoleic acid can also cause irritation and inflammation in high concentrations or with prolonged exposure. Therefore, medical definitions of this compound typically focus on its chemical structure and properties rather than its potential medicinal uses.

Ubiquinone, also known as coenzyme Q10 (CoQ10), is a lipid-soluble benzoquinone that plays a crucial role in the mitochondrial electron transport chain as an essential component of Complexes I, II, and III. It functions as an electron carrier, assisting in the transfer of electrons from reduced nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FADH2) to molecular oxygen during oxidative phosphorylation, thereby contributing to the generation of adenosine triphosphate (ATP), the primary energy currency of the cell.

Additionally, ubiquinone acts as a potent antioxidant in both membranes and lipoproteins, protecting against lipid peroxidation and oxidative damage to proteins and DNA. Its antioxidant properties stem from its ability to donate electrons and regenerate other antioxidants like vitamin E. Ubiquinone is synthesized endogenously in all human cells, with the highest concentrations found in tissues with high energy demands, such as the heart, liver, kidneys, and skeletal muscles.

Deficiency in ubiquinone can result from genetic disorders, aging, or certain medications (such as statins), leading to impaired mitochondrial function and increased oxidative stress. Supplementation with ubiquinone has been explored as a potential therapeutic strategy for various conditions associated with mitochondrial dysfunction and oxidative stress, including cardiovascular diseases, neurodegenerative disorders, and cancer.

Mycobacteriaceae is a family of gram-positive, aerobic bacteria that are characterized by their high content of mycolic acids in the cell wall. This family includes several medically important genera, most notably Mycobacterium and Mycobacteroides. Many species within this family are environmental organisms, found in soil and water, but some are significant human pathogens. They are known for their ability to resist decolorization by acid after being stained with a basic fuchsin stain, known as acid-fast bacilli (AFB). This property is due to the unique structure of their cell walls, which contain mycolic acids and other lipids that make them resistant to many chemical and physical agents.

Mycobacterium tuberculosis, the causative agent of tuberculosis (TB), is the most well-known pathogen within this family. Other important human pathogens include Mycobacterium leprae (leprosy), Mycobacterium avium complex (MAC) species that can cause pulmonary and disseminated infections, and Mycobacterium abscessus, which can cause various types of skin and soft tissue infections.

Mycobacteriaceae are typically slow-growing organisms, with some species taking weeks to grow in culture. Diagnosis of mycobacterial infections often involves microbiological culture, histopathology, and sometimes molecular techniques such as PCR and gene sequencing. Treatment usually requires a combination of antibiotics that target different components of the bacterial cell wall due to their inherent resistance to many conventional antibiotics.

Acetyl Coenzyme A, often abbreviated as Acetyl-CoA, is a key molecule in metabolism, particularly in the breakdown and oxidation of carbohydrates, fats, and proteins to produce energy. It is a coenzyme that plays a central role in the cellular process of transforming the energy stored in the chemical bonds of nutrients into a form that the cell can use.

Acetyl-CoA consists of an acetyl group (two carbon atoms) linked to coenzyme A, a complex organic molecule. This linkage is facilitated by an enzyme called acetyltransferase. Once formed, Acetyl-CoA can enter various metabolic pathways. In the citric acid cycle (also known as the Krebs cycle), Acetyl-CoA is further oxidized to release energy in the form of ATP, NADH, and FADH2, which are used in other cellular processes. Additionally, Acetyl-CoA is involved in the biosynthesis of fatty acids, cholesterol, and certain amino acids.

In summary, Acetyl Coenzyme A is a vital molecule in metabolism that connects various biochemical pathways for energy production and biosynthesis.

Hydroxymethylglutaryl CoA (HMG-CoA) reductase is an enzyme that plays a crucial role in the synthesis of cholesterol in the body. It is found in the endoplasmic reticulum of cells and catalyzes the conversion of HMG-CoA to mevalonic acid, which is a key rate-limiting step in the cholesterol biosynthetic pathway.

The reaction catalyzed by HMG-CoA reductase is as follows:

HMG-CoA + 2 NADPH + 2 H+ → mevalonic acid + CoA + 2 NADP+

This enzyme is the target of statin drugs, which are commonly prescribed to lower cholesterol levels in the treatment of cardiovascular diseases. Statins work by inhibiting HMG-CoA reductase, thereby reducing the production of cholesterol in the body.

Multiple Acyl Coenzyme A Dehydrogenase Deficiency (MADD) is a rare inherited metabolic disorder that affects the body's ability to break down certain fats and proteins. It is caused by mutations in genes that code for enzymes involved in the electron transfer flavoprotein-ubiquinone (ETF-QO) complex, which is responsible for transferring electrons from various acyl-CoA dehydrogenases to the electron transport chain during fatty acid and amino acid oxidation.

As a result of these genetic defects, there is a buildup of unoxidized acyl-CoA molecules in the body, leading to the accumulation of toxic intermediates that can damage organs and tissues. This can cause a wide range of symptoms, including hypoglycemia, metabolic acidosis, cardiac arrhythmias, muscle weakness, and developmental delays.

MADD is typically classified into three types based on the age of onset and severity of symptoms: neonatal, infantile, and late-onset. The neonatal form is the most severe and often leads to death in early infancy, while the infantile and late-onset forms can present with milder symptoms that may not become apparent until later in life.

Treatment for MADD typically involves a combination of dietary modifications, such as restricting long-chain fatty acids and supplementing with medium-chain triglycerides, and oral supplementation with riboflavin (vitamin B2), which has been shown to improve the activity of the ETF-QO complex in some cases.

Fatty acid desaturases are enzymes that introduce double bonds into fatty acid molecules, thereby reducing their saturation level. These enzymes play a crucial role in the synthesis of unsaturated fatty acids, which are essential components of cell membranes and precursors for various signaling molecules.

The position of the introduced double bond is specified by the type of desaturase enzyme. For example, Δ-9 desaturases introduce a double bond at the ninth carbon atom from the methyl end of the fatty acid chain. This enzyme is responsible for converting saturated fatty acids like stearic acid (18:0) to monounsaturated fatty acids like oleic acid (18:1n-9).

In humans, there are several fatty acid desaturases, including Δ-5 and Δ-6 desaturases, which introduce double bonds at the fifth and sixth carbon atoms from the methyl end, respectively. These enzymes are essential for the synthesis of long-chain polyunsaturated fatty acids (LC-PUFAs) such as arachidonic acid (20:4n-6), eicosapentaenoic acid (EPA, 20:5n-3), and docosahexaenoic acid (DHA, 22:6n-3).

Disorders in fatty acid desaturase activity or expression have been linked to various diseases, including cardiovascular disease, cancer, and metabolic disorders. Therefore, understanding the regulation and function of these enzymes is crucial for developing strategies to modulate fatty acid composition in cells and tissues, which may have therapeutic potential.

Palmitoyl-CoA hydrolase is an enzyme that catalyzes the hydrolysis of palmitoyl-coenzyme A (palmitoyl-CoA) to produce free coenzyme A (CoA) and palmitic acid. Palmitoyl-CoA is a fatty acyl-CoA ester that plays a central role in lipid metabolism, particularly in the synthesis of complex lipids such as triacylglycerols and phospholipids.

The reaction catalyzed by palmitoyl-CoA hydrolase is:

palmitoyl-CoA + H2O → CoA + palmitic acid

This enzyme is important for regulating the levels of palmitoyl-CoA in cells and may play a role in the development of metabolic disorders such as obesity and non-alcoholic fatty liver disease. Palmitoyl-CoA hydrolase has also been studied as a potential target for the development of therapies to treat these conditions.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Carbon-carbon ligases are a type of enzyme that catalyze the formation of carbon-carbon bonds between two molecules. These enzymes play important roles in various biological processes, including the biosynthesis of natural products and the metabolism of carbohydrates and lipids.

Carbon-carbon ligases can be classified into several categories based on the type of reaction they catalyze. For example, aldolases catalyze the condensation of an aldehyde or ketone with another molecule to form a new carbon-carbon bond and a new carbonyl group. Other examples include the polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs), which are large multienzyme complexes that catalyze the sequential addition of activated carbon units to form complex natural products.

Carbon-carbon ligases are important targets for drug discovery and development, as they play critical roles in the biosynthesis of many disease-relevant molecules. Inhibitors of these enzymes have shown promise as potential therapeutic agents for a variety of diseases, including cancer, infectious diseases, and metabolic disorders.

Triazenes are a class of organic compounds that contain a triazene functional group, which is composed of three nitrogen atoms bonded in a row (-N=N-NH-). In the context of medicine, certain triazene derivatives have been studied and used in cancer chemotherapy. For example, dacarbazine (also known as DTIC) is a triazene anticancer drug that is used to treat malignant melanoma and Hodgkin's lymphoma. These compounds are believed to work by alkylating DNA, which can disrupt cancer cell growth and division. However, their use is limited due to side effects and the development of resistance in some cases.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the body's energy production process. They are responsible for catalyzing the oxidation of various fatty acids, which are broken down into smaller molecules called acyl-CoAs in the body.

More specifically, acyl-CoA dehydrogenases facilitate the removal of electrons from the acyl-CoA molecules, which are then transferred to coenzyme Q10 and eventually to the electron transport chain. This process generates energy in the form of ATP, which is used by cells throughout the body for various functions.

There are several different types of acyl-CoA dehydrogenases, each responsible for oxidizing a specific type of acyl-CoA molecule. These include:

* Very long-chain acyl-CoA dehydrogenase (VLCAD), which oxidizes acyl-CoAs with 12 to 20 carbon atoms
* Long-chain acyl-CoA dehydrogenase (LCAD), which oxidizes acyl-CoAs with 14 to 20 carbon atoms
* Medium-chain acyl-CoA dehydrogenase (MCAD), which oxidizes acyl-CoAs with 6 to 12 carbon atoms
* Short-chain acyl-CoA dehydrogenase (SCAD), which oxidizes acyl-CoAs with 4 to 8 carbon atoms
* Isovaleryl-CoA dehydrogenase, which oxidizes isovaleryl-CoA, a specific type of branched-chain acyl-CoA molecule

Deficiencies in these enzymes can lead to various metabolic disorders, such as medium-chain acyl-CoA dehydrogenase deficiency (MCADD) or long-chain acyl-CoA dehydrogenase deficiency (LCADD), which can cause symptoms such as hypoglycemia, muscle weakness, and developmental delays.

Heterocyclic compounds are organic molecules that contain a ring structure made up of at least one atom that is not carbon, known as a heteroatom. These heteroatoms can include nitrogen, oxygen, sulfur, or other elements. In the case of "1-ring" heterocyclic compounds, the molecule contains a single ring structure composed of these heteroatoms and carbon atoms. Examples of 1-ring heterocyclic compounds include pyridine (contains one nitrogen atom in the ring), furan (contains one oxygen atom in the ring), and thiophene (contains one sulfur atom in the ring). These compounds play important roles in various biological processes and are also found in many drugs, dyes, and materials.

Cholesteryl esters are formed when cholesterol, a type of lipid (fat) that is important for the normal functioning of the body, becomes combined with fatty acids through a process called esterification. This results in a compound that is more hydrophobic (water-repelling) than cholesterol itself, which allows it to be stored more efficiently in the body.

Cholesteryl esters are found naturally in foods such as animal fats and oils, and they are also produced by the liver and other cells in the body. They play an important role in the structure and function of cell membranes, and they are also precursors to the synthesis of steroid hormones, bile acids, and vitamin D.

However, high levels of cholesteryl esters in the blood can contribute to the development of atherosclerosis, a condition characterized by the buildup of plaque in the arteries, which can increase the risk of heart disease and stroke. Cholesteryl esters are typically measured as part of a lipid profile, along with other markers such as total cholesterol, HDL cholesterol, and triglycerides.

A sterol esterase is an enzyme that catalyzes the hydrolysis of sterol esters, which are fatty acid esters of sterols (such as cholesterol) that are commonly found in lipoproteins and cell membranes. Sterol esterases play a crucial role in the metabolism of lipids by breaking down sterol esters into free sterols and free fatty acids, which can then be used in various biochemical processes.

There are several types of sterol esterases that have been identified, including:

1. Cholesteryl esterase (CE): This enzyme is responsible for hydrolyzing cholesteryl esters in the intestine and liver. It plays a critical role in the absorption and metabolism of dietary cholesterol.
2. Hormone-sensitive lipase (HSL): This enzyme is involved in the hydrolysis of sterol esters in adipose tissue, as well as other lipids such as triacylglycerols. It is regulated by hormones such as insulin and catecholamines.
3. Carboxylesterase (CES): This enzyme is a broad-specificity esterase that can hydrolyze various types of esters, including sterol esters. It is found in many tissues throughout the body.

Sterol esterases are important targets for drug development, as inhibiting these enzymes can have therapeutic effects in a variety of diseases, such as obesity, diabetes, and cardiovascular disease.

"Penicillium chrysogenum" is a species of filamentous fungi that is commonly found in the environment, particularly in soil and decaying vegetation. It is a member of the genus Penicillium, which includes several species that are known for their ability to produce penicillin, a group of antibiotics used to treat various bacterial infections.

"Penicillium chrysogenum" is one of the most important industrial producers of penicillin. It was originally identified as a separate species from "Penicillium notatum," which was the first species discovered to produce penicillin, but it is now considered to be a strain or variety of "Penicillium rubrum" or "Penicillium camemberti."

The fungus produces penicillin as a secondary metabolite, which means that it is not essential for the growth and development of the organism. Instead, penicillin is produced under certain conditions, such as nutrient limitation, to help the fungus compete with other microorganisms in its environment.

In addition to its medical importance, "Penicillium chrysogenum" also has industrial applications in the production of enzymes and other biomolecules. However, it can also cause food spoilage and allergic reactions in some individuals, so it is important to handle this organism with care.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Caprylates are the salts or esters of capric acid, a saturated fatty acid with a chain length of 8 carbon atoms. In medical and biological contexts, caprylate refers to the anion (negatively charged ion) form of capric acid, which has the chemical formula C8H17O2-. Caprylates are used in various applications, including as food additives, pharmaceuticals, and personal care products.

Some examples of caprylate compounds include:

* Sodium caprylate (sodium octanoate): a sodium salt commonly used as a preservative and flavor enhancer in foods.
* Calcium caprylate (calcium octanoate): a calcium salt used as an emulsifier in food products and as a stabilizer in cosmetics.
* Caprylic acid/caprylate triglycerides: esters of glycerin with caprylic acid, used as emollients and solvents in skin care products and pharmaceuticals.

Caprylates have antimicrobial properties against certain bacteria, fungi, and viruses, making them useful in various medical applications. For instance, sodium caprylate is sometimes used as an antifungal agent to treat conditions like candidiasis (yeast infections). However, more research is needed to fully understand the potential benefits and risks of using caprylates for medicinal purposes.

Glycerol-3-Phosphate O-Acyltransferase (GPAT) is an enzyme that plays a crucial role in the biosynthesis of triacylglycerols and phospholipids, which are major components of cellular membranes and energy storage molecules. The GPAT enzyme catalyzes the initial and rate-limiting step in the glycerolipid synthesis pathway, specifically the transfer of an acyl group from an acyl-CoA donor to the sn-1 position of glycerol-3-phosphate, forming lysophosphatidic acid (LPA). This reaction is essential for the production of various glycerolipids, including phosphatidic acid, diacylglycerol, and triacylglycerol. There are four isoforms of GPAT (GPAT1-4) in humans, each with distinct subcellular localizations and functions. Dysregulation of GPAT activity has been implicated in several pathological conditions, such as metabolic disorders, cardiovascular diseases, and cancers.

Cholesterol is a type of lipid (fat) molecule that is an essential component of cell membranes and is also used to make certain hormones and vitamins in the body. It is produced by the liver and is also obtained from animal-derived foods such as meat, dairy products, and eggs.

Cholesterol does not mix with blood, so it is transported through the bloodstream by lipoproteins, which are particles made up of both lipids and proteins. There are two main types of lipoproteins that carry cholesterol: low-density lipoproteins (LDL), also known as "bad" cholesterol, and high-density lipoproteins (HDL), also known as "good" cholesterol.

High levels of LDL cholesterol in the blood can lead to a buildup of cholesterol in the walls of the arteries, increasing the risk of heart disease and stroke. On the other hand, high levels of HDL cholesterol are associated with a lower risk of these conditions because HDL helps remove LDL cholesterol from the bloodstream and transport it back to the liver for disposal.

It is important to maintain healthy levels of cholesterol through a balanced diet, regular exercise, and sometimes medication if necessary. Regular screening is also recommended to monitor cholesterol levels and prevent health complications.

Esters are organic compounds that are formed by the reaction between an alcohol and a carboxylic acid. They are widely found in nature and are used in various industries, including the production of perfumes, flavors, and pharmaceuticals. In the context of medical definitions, esters may be mentioned in relation to their use as excipients in medications or in discussions of organic chemistry and biochemistry. Esters can also be found in various natural substances such as fats and oils, which are triesters of glycerol and fatty acids.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Coenzyme A-transferases are a group of enzymes that catalyze the transfer of Coenzyme A (CoA) from one molecule to another. CoA is a coenzyme that plays a crucial role in various metabolic processes, including the oxidation of carbohydrates, fatty acids, and amino acids.

Coenzyme A-transferases can be further classified into several subfamilies based on their specific functions and the types of molecules they act upon. For example, some CoA-transferases transfer CoA to acyl groups, forming acyl-CoAs, which are important intermediates in fatty acid metabolism. Other CoA-transferases transfer CoA to pyruvate, forming pyruvate dehydrogenase complexes that play a key role in glucose metabolism.

These enzymes are essential for maintaining the proper functioning of various metabolic pathways and are involved in a wide range of physiological processes, including energy production, lipid synthesis, and detoxification. Defects in CoA-transferases can lead to several metabolic disorders, such as fatty acid oxidation disorders and pyruvate dehydrogenase deficiency.

Esterification is a chemical reaction that involves the conversion of an alcohol and a carboxylic acid into an ester, typically through the removal of a molecule of water. This reaction is often catalyzed by an acid or a base, and it is a key process in organic chemistry. Esters are commonly found in nature and are responsible for the fragrances of many fruits and flowers. They are also important in the production of various industrial and consumer products, including plastics, resins, and perfumes.

Cobamides are a class of compounds that are structurally related to vitamin B12 (cobalamin). They consist of a corrin ring, which is a large heterocyclic ring made up of four pyrrole rings, and a cobalt ion in the center. The lower axial ligand of the cobalt ion can be a variety of different groups, including cyano, hydroxo, methyl, or 5'-deoxyadenosyl groups.

Cobamides are involved in a number of important biological processes, including the synthesis of amino acids and nucleotides, the metabolism of fatty acids and cholesterol, and the regulation of gene expression. They function as cofactors for enzymes called cobamide-dependent methyltransferases, which transfer methyl groups (CH3) from one molecule to another.

Cobamides are found in a wide variety of organisms, including bacteria, archaea, and eukaryotes. In humans, the most important cobamide is vitamin B12, which is essential for the normal functioning of the nervous system and the production of red blood cells. Vitamin B12 deficiency can lead to neurological problems and anemia.

Oleic acid is a monounsaturated fatty acid that is commonly found in various natural oils such as olive oil, sunflower oil, and grapeseed oil. Its chemical formula is cis-9-octadecenoic acid, and it is a colorless liquid at room temperature. Oleic acid is an important component of human diet and has been shown to have potential health benefits, including reducing the risk of heart disease and improving immune function. It is also used in the manufacture of soaps, cosmetics, and other personal care products.

Carboxylic ester hydrolases are a class of enzymes that catalyze the hydrolysis of ester bonds in carboxylic acid esters, producing alcohols and carboxylates. This group includes several subclasses of enzymes such as esterases, lipases, and thioesterases. These enzymes play important roles in various biological processes, including metabolism, detoxification, and signal transduction. They are widely used in industrial applications, such as the production of biodiesel, pharmaceuticals, and food ingredients.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Mesna is a medication used in the prevention and treatment of hemorrhagic cystitis (inflammation and bleeding of the bladder) caused by certain chemotherapy drugs, specifically ifosfamide and cyclophosphamide. Mesna works by neutralizing the toxic metabolites of these chemotherapy agents, which can cause bladder irritation and damage.

Mesna is administered intravenously (into a vein) along with ifosfamide or cyclophosphamide, and it may also be given as a separate infusion after the chemotherapy treatment. The dosage and timing of Mesna administration are determined by the healthcare provider based on the patient's weight, kidney function, and the dose of chemotherapy received.

It is important to note that Mesna does not have any direct anticancer effects and is used solely to manage the side effects of chemotherapy.

Oleic acid is a monounsaturated fatty acid that is commonly found in various natural oils such as olive oil, sunflower oil, and peanut oil. Its chemical formula is cis-9-octadecenoic acid, and it is a colorless liquid at room temperature with a slight odor. Oleic acid is an important component of human diet and has been shown to have various health benefits, including reducing the risk of heart disease and improving immune function. It is also used in the manufacture of soaps, cosmetics, and other industrial products.

Acylation is a medical and biological term that refers to the process of introducing an acyl group (-CO-) into a molecule. This process can occur naturally or it can be induced through chemical reactions. In the context of medicine and biology, acylation often occurs during post-translational modifications of proteins, where an acyl group is added to specific amino acid residues, altering the protein's function, stability, or localization.

An example of acylation in medicine is the administration of neuraminidase inhibitors, such as oseltamivir (Tamiflu), for the treatment and prevention of influenza. These drugs work by inhibiting the activity of the viral neuraminidase enzyme, which is essential for the release of newly formed virus particles from infected cells. Oseltamivir is administered orally as an ethyl ester prodrug, which is then hydrolyzed in the body to form the active acylated metabolite that inhibits the viral neuraminidase.

In summary, acylation is a vital process in medicine and biology, with implications for drug design, protein function, and post-translational modifications.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

Pantothenic Acid, also known as Vitamin B5, is a water-soluble vitamin that plays a vital role in the metabolism of proteins, carbohydrates, and fats. It is essential for the synthesis of coenzyme A (CoA), which is involved in various biochemical reactions in the body, including energy production, fatty acid synthesis, and cholesterol metabolism.

Pantothenic Acid is widely distributed in foods, including meat, poultry, fish, whole grains, legumes, and vegetables. Deficiency of this vitamin is rare but can lead to symptoms such as fatigue, irritability, sleep disturbances, muscle cramps, and gastrointestinal problems.

In addition to its role in metabolism, Pantothenic Acid also has potential benefits for wound healing, reducing inflammation, and supporting the immune system.

Microbodies are small, membrane-bound organelles found in the cells of eukaryotic organisms. They typically measure between 0.2 to 0.5 micrometers in diameter and play a crucial role in various metabolic processes, particularly in the detoxification of harmful substances and the synthesis of lipids.

There are several types of microbodies, including:

1. Peroxisomes: These are the most common type of microbody. They contain enzymes that help break down fatty acids and amino acids, producing hydrogen peroxide as a byproduct. Another set of enzymes within peroxisomes then converts the harmful hydrogen peroxide into water and oxygen, thus detoxifying the cell.
2. Glyoxysomes: These microbodies are primarily found in plants and some fungi. They contain enzymes involved in the glyoxylate cycle, a metabolic pathway that helps convert stored fats into carbohydrates during germination.
3. Microbody-like particles (MLPs): These are smaller organelles found in certain protists and algae. Their functions are not well understood but are believed to be involved in lipid metabolism.

It is important to note that microbodies do not have a uniform structure or function across all eukaryotic cells, and their specific roles can vary depending on the organism and cell type.

Pantetheine is not a medical term per se, but it is a biochemical compound with relevance to medicine. Pantetheine is the alcohol form of pantothenic acid (vitamin B5), and it plays a crucial role in the metabolism of proteins, carbohydrates, and fats. It is a component of coenzyme A, which is involved in numerous biochemical reactions within the body.

Coenzyme A, containing pantetheine, participates in oxidation-reduction reactions, energy production, and the synthesis of various compounds, such as fatty acids, cholesterol, steroid hormones, and neurotransmitters. Therefore, pantetheine is essential for maintaining proper cellular function and overall health.

While there isn't a specific medical condition associated with pantetheine deficiency, ensuring adequate intake of vitamin B5 (through diet or supplementation) is vital for optimal health and well-being.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Lipid metabolism is the process by which the body breaks down and utilizes lipids (fats) for various functions, such as energy production, cell membrane formation, and hormone synthesis. This complex process involves several enzymes and pathways that regulate the digestion, absorption, transport, storage, and consumption of fats in the body.

The main types of lipids involved in metabolism include triglycerides, cholesterol, phospholipids, and fatty acids. The breakdown of these lipids begins in the digestive system, where enzymes called lipases break down dietary fats into smaller molecules called fatty acids and glycerol. These molecules are then absorbed into the bloodstream and transported to the liver, which is the main site of lipid metabolism.

In the liver, fatty acids may be further broken down for energy production or used to synthesize new lipids. Excess fatty acids may be stored as triglycerides in specialized cells called adipocytes (fat cells) for later use. Cholesterol is also metabolized in the liver, where it may be used to synthesize bile acids, steroid hormones, and other important molecules.

Disorders of lipid metabolism can lead to a range of health problems, including obesity, diabetes, cardiovascular disease, and non-alcoholic fatty liver disease (NAFLD). These conditions may be caused by genetic factors, lifestyle habits, or a combination of both. Proper diagnosis and management of lipid metabolism disorders typically involves a combination of dietary changes, exercise, and medication.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Triglycerides are the most common type of fat in the body, and they're found in the food we eat. They're carried in the bloodstream to provide energy to the cells in our body. High levels of triglycerides in the blood can increase the risk of heart disease, especially in combination with other risk factors such as high LDL (bad) cholesterol, low HDL (good) cholesterol, and high blood pressure.

It's important to note that while triglycerides are a type of fat, they should not be confused with cholesterol, which is a waxy substance found in the cells of our body. Both triglycerides and cholesterol are important for maintaining good health, but high levels of either can increase the risk of heart disease.

Triglyceride levels are measured through a blood test called a lipid panel or lipid profile. A normal triglyceride level is less than 150 mg/dL. Borderline-high levels range from 150 to 199 mg/dL, high levels range from 200 to 499 mg/dL, and very high levels are 500 mg/dL or higher.

Elevated triglycerides can be caused by various factors such as obesity, physical inactivity, excessive alcohol consumption, smoking, and certain medical conditions like diabetes, hypothyroidism, and kidney disease. Medications such as beta-blockers, steroids, and diuretics can also raise triglyceride levels.

Lifestyle changes such as losing weight, exercising regularly, eating a healthy diet low in saturated and trans fats, avoiding excessive alcohol consumption, and quitting smoking can help lower triglyceride levels. In some cases, medication may be necessary to reduce triglycerides to recommended levels.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Euryarchaeota is a phylum within the domain Archaea, which consists of a diverse group of microorganisms that are commonly found in various environments such as soil, oceans, and the digestive tracts of animals. This group includes methanogens, which are archaea that produce methane as a metabolic byproduct, and extreme halophiles, which are archaea that thrive in highly saline environments.

The name Euryarchaeota comes from the Greek words "eury," meaning wide or broad, and "archaios," meaning ancient or primitive. This name reflects the phylum's diverse range of habitats and metabolic capabilities.

Euryarchaeota are characterized by their unique archaeal-type cell walls, which contain a variety of complex polysaccharides and proteins. They also have a distinct type of intracellular membrane called the archaellum, which is involved in motility. Additionally, Euryarchaeota have a unique genetic code that differs from that of bacteria and eukaryotes, with some codons specifying different amino acids.

Overall, Euryarchaeota are an important group of archaea that play a significant role in global carbon and nitrogen cycles, as well as in the breakdown of organic matter in various environments.

Propanediol Dehydratase is not a medical term per se, but rather a biochemical term. It refers to an enzyme that catalyzes the conversion of 1,2-propanediol (also known as propylene glycol) into propionaldehyde and water in the metabolic pathway known as the glycerol/propanediol utilization (GUD) system.

The reaction catalyzed by Propanediol Dehydratase is:
(CH3)2CH(OH)CH2OH → CH3CH2CHO + H2O

This enzyme is found in certain bacteria and archaea that are capable of utilizing 1,2-propanediol as a carbon source for growth. Deficiency or absence of this enzyme can affect the metabolic capabilities of these microorganisms.

Malonyl Coenzyme A (CoA) is not a medical term per se, but rather a biochemical concept. Here's the scientific or biochemical definition:

Malonyl Coenzyme A is an important intermediate in various metabolic pathways, particularly in fatty acid synthesis. It is formed through the reaction between malonic acid and coenzyme A, catalyzed by the enzyme acetyl-CoA carboxylase. Malonyl CoA plays a crucial role in the elongation step of fatty acid synthesis, where it provides the two-carbon unit that is added to a growing fatty acid chain.

In a medical context, understanding the function and regulation of Malonyl CoA metabolism can be relevant for several pathological conditions, including metabolic disorders like diabetes and obesity.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Acetate-CoA ligase is an enzyme that plays a role in the metabolism of acetate in cells. The enzyme catalyzes the conversion of acetate and coenzyme A (CoA) to acetyl-CoA, which is a key molecule in various metabolic pathways, including the citric acid cycle (also known as the Krebs cycle).

The reaction catalyzed by Acetate-CoA ligase can be summarized as follows:

acetate + ATP + CoA → acetyl-CoA + AMP + PPi

In this reaction, acetate is activated by combining it with ATP to form acetyl-AMP, which then reacts with CoA to produce acetyl-CoA. The reaction also produces AMP and pyrophosphate (PPi) as byproducts.

There are two main types of Acetate-CoA ligases: the short-chain fatty acid-CoA ligase, which is responsible for activating acetate and other short-chain fatty acids, and the acyl-CoA synthetase, which activates long-chain fatty acids. Both types of enzymes play important roles in energy metabolism and the synthesis of various biological molecules.

DNA Sequence Analysis is the systematic determination of the order of nucleotides in a DNA molecule. It is a critical component of modern molecular biology, genetics, and genetic engineering. The process involves determining the exact order of the four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - in a DNA molecule or fragment. This information is used in various applications such as identifying gene mutations, studying evolutionary relationships, developing molecular markers for breeding, and diagnosing genetic diseases.

The process of DNA Sequence Analysis typically involves several steps, including DNA extraction, PCR amplification (if necessary), purification, sequencing reaction, and electrophoresis. The resulting data is then analyzed using specialized software to determine the exact sequence of nucleotides.

In recent years, high-throughput DNA sequencing technologies have revolutionized the field of genomics, enabling the rapid and cost-effective sequencing of entire genomes. This has led to an explosion of genomic data and new insights into the genetic basis of many diseases and traits.

'Methanosarcina barkeri' is not a medical term, but a species name in the domain of microbiology. It refers to a type of archaea (single-celled organisms) that is capable of methanogenesis - producing methane as a metabolic byproduct. This microorganism is commonly found in anaerobic environments such as wetlands, digestive tracts of animals, and sewage sludge. It's not something that typically has a direct medical definition or relevance, unless in the context of specific research or environmental/industrial settings.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

Mevalonic acid is not a term that is typically used in medical definitions, but rather it is a biochemical concept. Mevalonic acid is a key intermediate in the biosynthetic pathway for cholesterol and other isoprenoids. It is formed from 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) by the enzyme HMG-CoA reductase, which is the target of cholesterol-lowering drugs known as statins.

In a medical context, mevalonic acid may be mentioned in relation to certain rare genetic disorders, such as mevalonate kinase deficiency (MKD) or hyperimmunoglobulinemia D and periodic fever syndrome (HIDS), which are caused by mutations in the gene encoding mevalonate kinase, an enzyme involved in the metabolism of mevalonic acid. These conditions can cause recurrent fevers, rashes, joint pain, and other symptoms.

Hydroxymethylglutaryl-CoA (HMG-CoA) reductase inhibitors, also known as statins, are a class of cholesterol-lowering medications. They work by inhibiting the enzyme HMG-CoA reductase, which plays a central role in the production of cholesterol in the liver. By blocking this enzyme, the liver is stimulated to take up more low-density lipoprotein (LDL) cholesterol from the bloodstream, leading to a decrease in LDL cholesterol levels and a reduced risk of cardiovascular disease.

Examples of HMG-CoA reductase inhibitors include atorvastatin, simvastatin, pravastatin, rosuvastatin, and fluvastatin. These medications are commonly prescribed to individuals with high cholesterol levels, particularly those who are at risk for or have established cardiovascular disease.

It's important to note that while HMG-CoA reductase inhibitors can be effective in reducing LDL cholesterol levels and the risk of cardiovascular events, they should be used as part of a comprehensive approach to managing high cholesterol, which may also include lifestyle modifications such as dietary changes, exercise, and weight management.

Riboflavin, also known as vitamin B2, is a water-soluble vitamin that plays a crucial role in energy production and cellular function, growth, and development. It is essential for the metabolism of carbohydrates, fats, and proteins, and it helps to maintain healthy skin, hair, and nails. Riboflavin is involved in the production of energy by acting as a coenzyme in various redox reactions. It also contributes to the maintenance of the mucous membranes of the digestive tract and promotes iron absorption.

Riboflavin can be found in a variety of foods, including milk, cheese, leafy green vegetables, liver, kidneys, legumes, yeast, mushrooms, and almonds. It is sensitive to light and heat, so exposure to these elements can lead to its degradation and loss of vitamin activity.

Deficiency in riboflavin is rare but can occur in individuals with poor dietary intake or malabsorption disorders. Symptoms of riboflavin deficiency include inflammation of the mouth and tongue, anemia, skin disorders, and neurological symptoms such as confusion and mood changes. Riboflavin supplements are available for those who have difficulty meeting their daily requirements through diet alone.

Methanobacterium is a genus of archaea belonging to the order Methanobacteriales and the family Methanobacteriaceae. They are commonly known as methanogenic bacteria, but they are not true bacteria; instead, they belong to the domain Archaea. These organisms are characterized by their ability to produce methane as a metabolic end-product in anaerobic conditions. They are typically found in environments like swamps, wetlands, digestive tracts of animals, and sewage sludge. The cells of Methanobacterium are usually rod-shaped and may appear gram-positive or gram-variable. Some species are capable of forming endospores.

Lovastatin is a medication that belongs to a class of drugs called statins, which are used to lower cholesterol levels in the blood. It works by inhibiting HMG-CoA reductase, an enzyme that plays a crucial role in the production of cholesterol in the body. By reducing the amount of cholesterol produced in the liver, lovastatin helps to decrease the levels of low-density lipoprotein (LDL) or "bad" cholesterol and triglycerides in the blood, while increasing the levels of high-density lipoprotein (HDL) or "good" cholesterol.

Lovastatin is available in both immediate-release and extended-release forms, and it is typically taken orally once or twice a day, depending on the dosage prescribed by a healthcare provider. Common side effects of lovastatin include headache, nausea, diarrhea, and muscle pain, although more serious side effects such as liver damage and muscle weakness are possible, particularly at higher doses.

It is important to note that lovastatin should not be taken by individuals with active liver disease or by those who are pregnant or breastfeeding. Additionally, it may interact with certain other medications, so it is essential to inform a healthcare provider of all medications being taken before starting lovastatin therapy.

Phosphatidylcholines (PtdCho) are a type of phospholipids that are essential components of cell membranes in living organisms. They are composed of a hydrophilic head group, which contains a choline moiety, and two hydrophobic fatty acid chains. Phosphatidylcholines are crucial for maintaining the structural integrity and function of cell membranes, and they also serve as important precursors for the synthesis of signaling molecules such as acetylcholine. They can be found in various tissues and biological fluids, including blood, and are abundant in foods such as soybeans, eggs, and meat. Phosphatidylcholines have been studied for their potential health benefits, including their role in maintaining healthy lipid metabolism and reducing the risk of cardiovascular disease.

Macrophages are a type of white blood cell that are an essential part of the immune system. They are large, specialized cells that engulf and destroy foreign substances, such as bacteria, viruses, parasites, and fungi, as well as damaged or dead cells. Macrophages are found throughout the body, including in the bloodstream, lymph nodes, spleen, liver, lungs, and connective tissues. They play a critical role in inflammation, immune response, and tissue repair and remodeling.

Macrophages originate from monocytes, which are a type of white blood cell produced in the bone marrow. When monocytes enter the tissues, they differentiate into macrophages, which have a larger size and more specialized functions than monocytes. Macrophages can change their shape and move through tissues to reach sites of infection or injury. They also produce cytokines, chemokines, and other signaling molecules that help coordinate the immune response and recruit other immune cells to the site of infection or injury.

Macrophages have a variety of surface receptors that allow them to recognize and respond to different types of foreign substances and signals from other cells. They can engulf and digest foreign particles, bacteria, and viruses through a process called phagocytosis. Macrophages also play a role in presenting antigens to T cells, which are another type of immune cell that helps coordinate the immune response.

Overall, macrophages are crucial for maintaining tissue homeostasis, defending against infection, and promoting wound healing and tissue repair. Dysregulation of macrophage function has been implicated in a variety of diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions.

Acetates, in a medical context, most commonly refer to compounds that contain the acetate group, which is an functional group consisting of a carbon atom bonded to two hydrogen atoms and an oxygen atom (-COO-). An example of an acetate is sodium acetate (CH3COONa), which is a salt formed from acetic acid (CH3COOH) and is often used as a buffering agent in medical solutions.

Acetates can also refer to a group of medications that contain acetate as an active ingredient, such as magnesium acetate, which is used as a laxative, or calcium acetate, which is used to treat high levels of phosphate in the blood.

In addition, acetates can also refer to a process called acetylation, which is the addition of an acetyl group (-COCH3) to a molecule. This process can be important in the metabolism and regulation of various substances within the body.

Molecular structure, in the context of biochemistry and molecular biology, refers to the arrangement and organization of atoms and chemical bonds within a molecule. It describes the three-dimensional layout of the constituent elements, including their spatial relationships, bond lengths, and angles. Understanding molecular structure is crucial for elucidating the functions and reactivities of biological macromolecules such as proteins, nucleic acids, lipids, and carbohydrates. Various experimental techniques, like X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM), are employed to determine molecular structures at atomic resolution, providing valuable insights into their biological roles and potential therapeutic targets.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Phospholipids are a major class of lipids that consist of a hydrophilic (water-attracting) head and two hydrophobic (water-repelling) tails. The head is composed of a phosphate group, which is often bound to an organic molecule such as choline, ethanolamine, serine or inositol. The tails are made up of two fatty acid chains.

Phospholipids are a key component of cell membranes and play a crucial role in maintaining the structural integrity and function of the cell. They form a lipid bilayer, with the hydrophilic heads facing outwards and the hydrophobic tails facing inwards, creating a barrier that separates the interior of the cell from the outside environment.

Phospholipids are also involved in various cellular processes such as signal transduction, intracellular trafficking, and protein function regulation. Additionally, they serve as emulsifiers in the digestive system, helping to break down fats in the diet.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Hydroxymethylglutaryl-CoA-Reductases (NADP-dependent) are a group of enzymes that play a crucial role in the metabolic pathway known as cholesterol biosynthesis. The NADP-dependent hydroxymethylglutaryl-CoA reductase (HMGCR) is the rate-limiting enzyme in this pathway, and it catalyzes the conversion of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) to mevalonic acid using nicotinamide adenine dinucleotide phosphate (NADPH) as a cofactor.

Mevalonic acid is a key intermediate in the biosynthesis of cholesterol and other isoprenoids, making HMGCR an important target for cholesterol-lowering drugs such as statins. Mutations in the gene encoding HMGCR can lead to several genetic disorders, including megacephaly-capillary malformation syndrome and cerebrotendinous xanthomatosis.

Methylmalonyl-CoA mutase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, which is an important step in the catabolic pathways of valine, isoleucine, threonine, methionine, odd-chain fatty acids, and cholesterol.

The enzyme requires a cofactor called adenosylcobalamin (vitamin B12) for its activity. In the absence of this cofactor or due to mutations in the gene encoding the enzyme, methylmalonyl-CoA mutase deficiency can occur, leading to the accumulation of methylmalonic acid and other toxic metabolites, which can cause a range of symptoms including vomiting, dehydration, lethargy, hypotonia, developmental delay, and metabolic acidosis. This condition is typically inherited in an autosomal recessive manner and can be diagnosed through biochemical tests and genetic analysis.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Methane is not a medical term, but it is a chemical compound that is often mentioned in the context of medicine and health. Medically, methane is significant because it is one of the gases produced by anaerobic microorganisms during the breakdown of organic matter in the gut, leading to conditions such as bloating, cramping, and diarrhea. Excessive production of methane can also be a symptom of certain digestive disorders like irritable bowel syndrome (IBS) and small intestinal bacterial overgrowth (SIBO).

In broader terms, methane is a colorless, odorless gas that is the primary component of natural gas. It is produced naturally by the decomposition of organic matter in anaerobic conditions, such as in landfills, wetlands, and the digestive tracts of animals like cows and humans. Methane is also a potent greenhouse gas with a global warming potential 25 times greater than carbon dioxide over a 100-year time frame.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Aldehyde oxidoreductases are a class of enzymes that catalyze the oxidation of aldehydes to carboxylic acids using NAD+ or FAD as cofactors. They play a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. These enzymes are widely distributed in nature and have been identified in bacteria, yeast, plants, and animals.

The oxidation reaction catalyzed by aldehyde oxidoreductases involves the transfer of electrons from the aldehyde substrate to the cofactor, resulting in the formation of a carboxylic acid and reduced NAD+ or FAD. The enzymes are classified into several families based on their sequence similarity and cofactor specificity.

One of the most well-known members of this family is alcohol dehydrogenase (ADH), which catalyzes the oxidation of alcohols to aldehydes or ketones as part of the alcohol metabolism pathway. Another important member is aldehyde dehydrogenase (ALDH), which further oxidizes the aldehydes generated by ADH to carboxylic acids, thereby preventing the accumulation of toxic aldehydes in the body.

Deficiencies in ALDH enzymes have been linked to several human diseases, including alcoholism and certain types of cancer. Therefore, understanding the structure and function of aldehyde oxidoreductases is essential for developing new therapeutic strategies to treat these conditions.

Oxo-acid lyases are a class of enzymes that catalyze the cleavage of a carbon-carbon bond in an oxo-acid to give a molecule with a carbonyl group and a carbanion, which then reacts non-enzymatically with a proton to form a new double bond. The reaction is reversible, and the enzyme can also catalyze the reverse reaction.

Oxo-acid lyases play important roles in various metabolic pathways, such as the citric acid cycle, glyoxylate cycle, and the degradation of certain amino acids. These enzymes are characterized by the presence of a conserved catalytic mechanism involving a nucleophilic attack on the carbonyl carbon atom of the oxo-acid substrate.

The International Union of Biochemistry and Molecular Biology (IUBMB) has classified oxo-acid lyases under EC 4.1.3, which includes enzymes that catalyze the formation of a carbon-carbon bond by means other than carbon-carbon bond formation to an enolate or carbonion, a carbanionic fragment, or a Michael acceptor.

Molecular conformation, also known as spatial arrangement or configuration, refers to the specific three-dimensional shape and orientation of atoms that make up a molecule. It describes the precise manner in which bonds between atoms are arranged around a molecular framework, taking into account factors such as bond lengths, bond angles, and torsional angles.

Conformational isomers, or conformers, are different spatial arrangements of the same molecule that can interconvert without breaking chemical bonds. These isomers may have varying energies, stability, and reactivity, which can significantly impact a molecule's biological activity and function. Understanding molecular conformation is crucial in fields such as drug design, where small changes in conformation can lead to substantial differences in how a drug interacts with its target.

Corrinoids are a class of compounds that include vitamin B12 and its analogs. Vitamin B12 is an essential nutrient for humans and other animals, playing a critical role in the synthesis of DNA, the maintenance of the nervous system, and the metabolism of fatty acids and amino acids.

The corrinoid ring is the structural backbone of vitamin B12 and its analogs. It is a complex, planar molecule made up of four pyrrole rings joined together in a macrocycle. The corrinoid ring contains a central cobalt ion, which can form coordination bonds with various ligands, including organic groups such as methyl, hydroxo, and cyano.

Corrinoids can be found in a wide variety of foods, including meat, dairy products, fish, eggs, and some fortified plant-based foods. They are also produced by certain bacteria, which can synthesize the corrinoid ring and the cobalt ion de novo. Some corrinoids have biological activity similar to vitamin B12, while others do not.

In addition to their role in human nutrition, corrinoids are also used in industrial applications, such as the production of antibiotics and other pharmaceuticals. They are also used as catalysts in chemical reactions, due to their ability to form stable coordination complexes with various ligands.

Simvastatin is a medication that belongs to a class of drugs called statins, which are used to lower cholesterol levels in the blood. It works by inhibiting HMG-CoA reductase, an enzyme that plays a key role in the production of cholesterol in the body. By reducing the amount of cholesterol produced by the liver, simvastatin helps to lower the levels of LDL (low-density lipoprotein) or "bad" cholesterol and triglycerides in the blood, while increasing HDL (high-density lipoprotein) or "good" cholesterol.

Simvastatin is used to prevent cardiovascular diseases such as heart attacks and strokes in individuals with high cholesterol levels, particularly those who have other risk factors such as diabetes, hypertension, or a history of smoking. It is available in various strengths and forms, and is typically taken orally once a day, usually in the evening.

Like all medications, simvastatin can cause side effects, ranging from mild to severe. Common side effects include headache, muscle pain, and gastrointestinal symptoms such as nausea, constipation, or diarrhea. Rare but serious side effects may include liver damage, muscle breakdown (rhabdomyolysis), and increased risk of diabetes. It is important to follow the dosage instructions carefully and inform your healthcare provider of any pre-existing medical conditions or medications you are taking, as these may affect the safety and efficacy of simvastatin.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Vitamin B12, also known as cobalamin, is a water-soluble vitamin that plays a crucial role in the synthesis of DNA, formation of red blood cells, and maintenance of the nervous system. It is involved in the metabolism of every cell in the body, particularly affecting DNA regulation and neurological function.

Vitamin B12 is unique among vitamins because it contains a metal ion, cobalt, from which its name is derived. This vitamin can be synthesized only by certain types of bacteria and is not produced by plants or animals. The major sources of vitamin B12 in the human diet include animal-derived foods such as meat, fish, poultry, eggs, and dairy products, as well as fortified plant-based milk alternatives and breakfast cereals.

Deficiency in vitamin B12 can lead to various health issues, including megaloblastic anemia, fatigue, neurological symptoms such as numbness and tingling in the extremities, memory loss, and depression. Since vitamin B12 is not readily available from plant-based sources, vegetarians and vegans are at a higher risk of deficiency and may require supplementation or fortified foods to meet their daily requirements.

Phosphate Acetyltransferase (PAT) is an enzyme involved in the metabolism of certain amino acids. It catalyzes the transfer of a phosphate group from acetyl phosphate to a variety of acceptor molecules, including carbon, nitrogen, and sulfur nucleophiles. This reaction plays a crucial role in several biochemical pathways, such as the biosynthesis of certain amino acids, vitamins, and cofactors.

The systematic name for this enzyme is acetylphosphate-protein phosphotransferase. It belongs to the family of transferases, specifically those transferring phosphorus-containing groups. The gene that encodes this enzyme in humans is called PAT1 or CABYR. Defects in this gene have been associated with certain neurological disorders.

Acetyltransferases are a type of enzyme that facilitates the transfer of an acetyl group (a chemical group consisting of an acetyl molecule, which is made up of carbon, hydrogen, and oxygen atoms) from a donor molecule to a recipient molecule. This transfer of an acetyl group can modify the function or activity of the recipient molecule.

In the context of biology and medicine, acetyltransferases are important for various cellular processes, including gene expression, DNA replication, and protein function. For example, histone acetyltransferases (HATs) are a type of acetyltransferase that add an acetyl group to the histone proteins around which DNA is wound. This modification can alter the structure of the chromatin, making certain genes more or less accessible for transcription, and thereby influencing gene expression.

Abnormal regulation of acetyltransferases has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the function and regulation of these enzymes is an important area of research in biomedicine.

Fatty acid synthase type II (FASN2) is an alternative form of fatty acid synthase, which is a multi-functional enzyme complex responsible for the de novo synthesis of palmitate, a 16-carbon saturated fatty acid. In contrast to the classical type I fatty acid synthase (FASN), which is found in the cytoplasm and exists as a homodimer, FASN2 is localized in the mitochondria and consists of individual, monofunctional enzymes that catalyze each step of the fatty acid synthesis process.

The type II fatty acid synthase system includes several enzymes: acetyl-CoA carboxylase (ACC), which provides malonyl-CoA; 3-ketoacyl-CoA thiolase, which catalyzes the initial condensation of acetyl-CoA and malonyl-CoA to form acetoacetyl-CoA; 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (HAD), which catalyzes the reduction, dehydration, and isomerization of acetoacetyl-CoA to form hydroxybutyryl-CoA; 3-ketoacyl-CoA reductase, which reduces hydroxybutyryl-CoA to butyryl-CoA; and enoyl-CoA reductase (ECR), which catalyzes the final reduction of butyryl-CoA to palmitate.

FASN2 is involved in various cellular processes, including energy metabolism, lipid biosynthesis, and protein acetylation. Dysregulation of FASN2 has been implicated in several diseases, such as cancer, obesity, and neurodegenerative disorders.

Sterols are a type of organic compound that is derived from steroids and found in the cell membranes of organisms. In animals, including humans, cholesterol is the most well-known sterol. Sterols help to maintain the structural integrity and fluidity of cell membranes, and they also play important roles as precursors for the synthesis of various hormones and other signaling molecules. Phytosterols are plant sterols that have been shown to have cholesterol-lowering effects in humans when consumed in sufficient amounts.

Flavin-Adenine Dinucleotide (FAD) is a coenzyme that plays a crucial role in various metabolic processes, particularly in the electron transport chain where it functions as an electron carrier in oxidation-reduction reactions. FAD is composed of a flavin moiety, riboflavin or vitamin B2, and adenine dinucleotide. It can exist in two forms: an oxidized form (FAD) and a reduced form (FADH2). The reduction of FAD to FADH2 involves the gain of two electrons and two protons, which is accompanied by a significant conformational change that allows FADH2 to donate its electrons to subsequent components in the electron transport chain, ultimately leading to the production of ATP, the main energy currency of the cell.

Thiol esters are chemical compounds that contain a sulfur atom (from a mercapto group, -SH) linked to a carbonyl group (a carbon double-bonded to an oxygen atom, -CO-) through an ester bond. Thiolester hydrolases are enzymes that catalyze the hydrolysis of thiol esters, breaking down these compounds into a carboxylic acid and a thiol (a compound containing a mercapto group).

In biological systems, thiolester bonds play important roles in various metabolic pathways. For example, acetyl-CoA, a crucial molecule in energy metabolism, is a thiol ester that forms between coenzyme A and an acetyl group. Thiolester hydrolases help regulate the formation and breakdown of these thiol esters, allowing cells to control various biochemical reactions.

Examples of thiolester hydrolases include:

1. CoA thioesterases (CoATEs): These enzymes hydrolyze thiol esters between coenzyme A and fatty acids, releasing free coenzyme A and a fatty acid. This process is essential for fatty acid metabolism.
2. Acetyl-CoA hydrolase: This enzyme specifically breaks down the thiol ester bond in acetyl-CoA, releasing acetic acid and coenzyme A.
3. Thioesterases involved in non-ribosomal peptide synthesis (NRPS): These enzymes hydrolyze thiol esters during the biosynthesis of complex peptides, allowing for the formation of unique amino acid sequences and structures.

Understanding the function and regulation of thiolester hydrolases can provide valuable insights into various metabolic processes and potential therapeutic targets in disease treatment.

Thin-layer chromatography (TLC) is a type of chromatography used to separate, identify, and quantify the components of a mixture. In TLC, the sample is applied as a small spot onto a thin layer of adsorbent material, such as silica gel or alumina, which is coated on a flat, rigid support like a glass plate. The plate is then placed in a developing chamber containing a mobile phase, typically a mixture of solvents.

As the mobile phase moves up the plate by capillary action, it interacts with the stationary phase and the components of the sample. Different components of the mixture travel at different rates due to their varying interactions with the stationary and mobile phases, resulting in distinct spots on the plate. The distance each component travels can be measured and compared to known standards to identify and quantify the components of the mixture.

TLC is a simple, rapid, and cost-effective technique that is widely used in various fields, including forensics, pharmaceuticals, and research laboratories. It allows for the separation and analysis of complex mixtures with high resolution and sensitivity, making it an essential tool in many analytical applications.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Fatty acid synthases (FAS) are a group of enzymes that are responsible for the synthesis of fatty acids in the body. They catalyze a series of reactions that convert acetyl-CoA and malonyl-CoA into longer chain fatty acids, which are then used for various purposes such as energy storage or membrane formation.

The human genome encodes two types of FAS: type I and type II. Type I FAS is a large multifunctional enzyme complex found in the cytoplasm of cells, while type II FAS consists of individual enzymes located in the mitochondria. Both types of FAS play important roles in lipid metabolism, but their regulation and expression differ depending on the tissue and physiological conditions.

Inhibition of FAS has been explored as a potential therapeutic strategy for various diseases, including cancer, obesity, and metabolic disorders. However, more research is needed to fully understand the complex mechanisms regulating FAS activity and its role in human health and disease.

Acyl-Carrier Protein S-Malonyltransferase is an enzyme that plays a crucial role in the biosynthesis of fatty acids. The systematic name for this enzyme is 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH).

The enzyme catalyzes the following reaction:
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]

This reaction is part of the fatty acid synthase complex, which is responsible for the synthesis of long-chain fatty acids. The enzyme transfers a malonyl group from malonyl-CoA to an acyl carrier protein (ACP), which acts as a cofactor in the reaction. This transfer forms a malonyl-ACP, which is then used as a building block for the synthesis of fatty acids.

The enzyme is found in bacteria, plants, and animals, including humans. In humans, it is encoded by the MAT1A gene and is primarily located in the liver, where it plays a role in the production of palmitate, a 16-carbon saturated fatty acid that is an important precursor for the synthesis of other lipids.

Deficiencies in Acyl-Carrier Protein S-Malonyltransferase have been associated with various metabolic disorders, including cardiovascular disease and nonalcoholic fatty liver disease.

Mercaptoethanol, also known as β-mercaptoethanol or BME, is not a medical term itself but is commonly used in laboratories including medical research. It is a reducing agent and a powerful antioxidant with the chemical formula HOCH2CH2SH.

Medical Definition:
Mercaptoethanol (β-mercaptoethanol) is a colorless liquid with an unpleasant odor, used as a reducing agent in biochemical research and laboratory experiments. It functions by breaking disulfide bonds between cysteine residues in proteins, allowing them to unfold and denature. This property makes it useful for various applications such as protein purification, enzyme assays, and cell culture.

However, it is important to note that Mercaptoethanol has a high toxicity level and should be handled with caution in the laboratory setting.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Methanosarcina is a genus of archaea, which are single-celled microorganisms that lack a nucleus and other membrane-bound organelles. These archaea are characterized by their ability to produce methane as a metabolic byproduct during the process of anaerobic respiration or fermentation. Methanosarcina species are found in various environments, including freshwater and marine sediments, waste treatment facilities, and the digestive tracts of animals. They are capable of degrading a wide range of organic compounds, such as acetate, methanol, and methylamines, to produce methane. It's important to note that while Methanosarcina species can be beneficial in certain environments, they may also contribute to the release of greenhouse gases, particularly methane, which is a potent contributor to climate change.

Hydroxymethylglutaryl-CoA Synthase (HMG-CoA Synthase) is a key enzyme in the cholesterol biosynthesis pathway. It catalyzes the reaction of acetoacetyl-CoA and acetyl-CoA to form HMG-CoA (3-hydroxy-3-methylglutaryl-coenzyme A), which is a crucial intermediate in the synthesis of cholesterol, ketone bodies, and other isoprenoids.

There are two isoforms of this enzyme: HMG-CoA synthase 1 (HMGCS1) and HMG-CoA synthase 2 (HMGCS2). HMGCS1 is primarily expressed in the liver and is involved in cholesterol synthesis, while HMGCS2 is mainly found in the brain, kidney, and liver, where it plays a role in ketone body synthesis during periods of fasting or low-carbohydrate diets.

Defects in HMG-CoA synthase can lead to metabolic disorders, such as hypocholesterolemia (low cholesterol levels) and hyperketonemia (elevated ketone bodies). Additionally, inhibitors of HMG-CoA synthase are used as cholesterol-lowering drugs, known as statins, to treat conditions like hyperlipidemia and prevent cardiovascular diseases.

Phosphatidylethanolamines (PE) are a type of phospholipid that are abundantly found in the cell membranes of living organisms. They play a crucial role in maintaining the structural integrity and functionality of the cell membrane. PE contains a hydrophilic head, which consists of an ethanolamine group linked to a phosphate group, and two hydrophobic fatty acid chains. This unique structure allows PE to form a lipid bilayer, where the hydrophilic heads face outwards and interact with the aqueous environment, while the hydrophobic tails face inwards and interact with each other.

PE is also involved in various cellular processes, such as membrane trafficking, autophagy, and signal transduction. Additionally, PE can be modified by the addition of various functional groups or molecules, which can further regulate its functions and interactions within the cell. Overall, phosphatidylethanolamines are essential components of cellular membranes and play a critical role in maintaining cellular homeostasis.

Methyltransferases are a class of enzymes that catalyze the transfer of a methyl group (-CH3) from a donor molecule to an acceptor molecule, which is often a protein, DNA, or RNA. This transfer of a methyl group can modify the chemical and physical properties of the acceptor molecule, playing a crucial role in various cellular processes such as gene expression, signal transduction, and DNA repair.

In biochemistry, methyltransferases are classified based on the type of donor molecule they use for the transfer of the methyl group. The most common methyl donor is S-adenosylmethionine (SAM), a universal methyl group donor found in many organisms. Methyltransferases that utilize SAM as a cofactor are called SAM-dependent methyltransferases.

Abnormal regulation or function of methyltransferases has been implicated in several diseases, including cancer and neurological disorders. Therefore, understanding the structure, function, and regulation of these enzymes is essential for developing targeted therapies to treat these conditions.

Ethanolamine ammonia-lyase (EAL) is an enzyme that plays a role in the breakdown and metabolism of certain compounds in the body. Its primary function is to catalyze the conversion of ethanolamine, a type of amino alcohol, into acetaldehyde and ammonia. This reaction is an important step in the catabolism of phosphatidylethanolamines, which are major components of cell membranes.

EAL is also known as "ethanolamine deaminase" or "N-ethanolamine deaminase." It requires the cofactor pyridoxal phosphate (PLP) to facilitate the reaction. The enzyme's activity has been identified in various organisms, including bacteria, archaea, and plants, but not in mammals. In some bacterial species, EAL is involved in the biosynthesis of certain amino acids and other biomolecules.

The reaction catalyzed by ethanolamine ammonia-lyase:

Ethanolamine + H2O + PLP → Acetaldehyde + Ammonia + Methylglyoxal + PLP

An apoenzyme is the protein component of an enzyme that is responsible for its catalytic activity. It combines with a cofactor, which can be either an organic or inorganic non-protein molecule, to form the active enzyme. The cofactor can be a metal ion or a small organic molecule called a coenzyme.

The term "apoenzyme" is used to describe the protein portion of an enzyme after it has lost its cofactor. When the apoenzyme combines with the cofactor, the active holoenzyme is formed, which is capable of carrying out the specific biochemical reaction for which the enzyme is responsible.

In some cases, the loss of a cofactor can result in the complete loss of enzymatic activity, while in other cases, the apoenzyme may retain some residual activity. The relationship between an apoenzyme and its cofactor is specific, meaning that each cofactor typically only binds to and activates one particular type of apoenzyme.

Membrane lipids are the main component of biological membranes, forming a lipid bilayer in which various cellular processes take place. These lipids include phospholipids, glycolipids, and cholesterol. Phospholipids are the most abundant type, consisting of a hydrophilic head (containing a phosphate group) and two hydrophobic tails (composed of fatty acid chains). Glycolipids contain a sugar group attached to the lipid molecule. Cholesterol helps regulate membrane fluidity and permeability. Together, these lipids create a selectively permeable barrier that separates cells from their environment and organelles within cells.

A chemical model is a simplified representation or description of a chemical system, based on the laws of chemistry and physics. It is used to explain and predict the behavior of chemicals and chemical reactions. Chemical models can take many forms, including mathematical equations, diagrams, and computer simulations. They are often used in research, education, and industry to understand complex chemical processes and develop new products and technologies.

For example, a chemical model might be used to describe the way that atoms and molecules interact in a particular reaction, or to predict the properties of a new material. Chemical models can also be used to study the behavior of chemicals at the molecular level, such as how they bind to each other or how they are affected by changes in temperature or pressure.

It is important to note that chemical models are simplifications of reality and may not always accurately represent every aspect of a chemical system. They should be used with caution and validated against experimental data whenever possible.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Palmitic acid is a type of saturated fatty acid, which is a common component in many foods and also produced by the body. Its chemical formula is C16:0, indicating that it contains 16 carbon atoms and no double bonds. Palmitic acid is found in high concentrations in animal fats, such as butter, lard, and beef tallow, as well as in some vegetable oils, like palm kernel oil and coconut oil.

In the human body, palmitic acid can be synthesized from other substances or absorbed through the diet. It plays a crucial role in various biological processes, including energy storage, membrane structure formation, and signaling pathways regulation. However, high intake of palmitic acid has been linked to an increased risk of developing cardiovascular diseases due to its potential to raise low-density lipoprotein (LDL) cholesterol levels in the blood.

It is essential to maintain a balanced diet and consume palmitic acid-rich foods in moderation, along with regular exercise and a healthy lifestyle, to reduce the risk of chronic diseases.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

A lipid bilayer is a thin membrane made up of two layers of lipid molecules, primarily phospholipids. The hydrophilic (water-loving) heads of the lipids face outwards, coming into contact with watery environments on both sides, while the hydrophobic (water-fearing) tails point inward, away from the aqueous surroundings. This unique structure allows lipid bilayers to form a stable barrier that controls the movement of molecules and ions in and out of cells and organelles, thus playing a crucial role in maintaining cellular compartmentalization and homeostasis.

Carnitine is a naturally occurring substance in the body that plays a crucial role in energy production. It transports long-chain fatty acids into the mitochondria, where they can be broken down to produce energy. Carnitine is also available as a dietary supplement and is often used to treat or prevent carnitine deficiency.

The medical definition of Carnitine is:

"A quaternary ammonium compound that occurs naturally in animal tissues, especially in muscle, heart, brain, and liver. It is essential for the transport of long-chain fatty acids into the mitochondria, where they can be oxidized to produce energy. Carnitine also functions as an antioxidant and has been studied as a potential treatment for various conditions, including heart disease, diabetes, and kidney disease."

Carnitine is also known as L-carnitine or levocarnitine. It can be found in foods such as red meat, dairy products, fish, poultry, and tempeh. In the body, carnitine is synthesized from the amino acids lysine and methionine with the help of vitamin C and iron. Some people may have a deficiency in carnitine due to genetic factors, malnutrition, or certain medical conditions, such as kidney disease or liver disease. In these cases, supplementation may be necessary to prevent or treat symptoms of carnitine deficiency.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

Glutarates are compounds that contain a glutaric acid group. Glutaric acid is a carboxylic acid with a five-carbon chain and two carboxyl groups at the 1st and 5th carbon positions. Glutarates can be found in various substances, including certain foods and medications.

In a medical context, glutarates are sometimes used as ingredients in pharmaceutical products. For example, sodium phenylbutyrate, which is a salt of phenylbutyric acid and butyric acid, contains a glutaric acid group and is used as a medication to treat urea cycle disorders.

Glutarates can also be found in some metabolic pathways in the body, where they play a role in energy production and other biochemical processes. However, abnormal accumulation of glutaric acid or its derivatives can lead to certain medical conditions, such as glutaric acidemia type I, which is an inherited disorder of metabolism that can cause neurological symptoms and other health problems.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Lipids are a broad group of organic compounds that are insoluble in water but soluble in nonpolar organic solvents. They include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E, and K), monoglycerides, diglycerides, triglycerides, and phospholipids. Lipids serve many important functions in the body, including energy storage, acting as structural components of cell membranes, and serving as signaling molecules. High levels of certain lipids, particularly cholesterol and triglycerides, in the blood are associated with an increased risk of cardiovascular disease.

Differential scanning calorimetry (DSC) is a thermoanalytical technique used to measure the difference in the amount of heat required to increase the temperature of a sample and a reference as a function of temperature. It is commonly used to study phase transitions, such as melting, crystallization, and glass transition, as well as chemical reactions, in a wide range of materials, including polymers, pharmaceuticals, and biological samples.

In DSC, the sample and reference are placed in separate pans and heated at a constant rate. The heat flow required to maintain this heating rate is continuously measured for both the sample and the reference. As the temperature of the sample changes during a phase transition or chemical reaction, the heat flow required to maintain the same heating rate will change relative to the reference. This allows for the measurement of the enthalpy change (ΔH) associated with the transition or reaction.

Differential scanning calorimetry is a powerful tool in materials science and research as it can provide information about the thermal behavior, stability, and composition of materials. It can also be used to study the kinetics of reactions and phase transitions, making it useful for optimizing processing conditions and developing new materials.

'Clostridium' is a genus of gram-positive, rod-shaped bacteria that are widely distributed in nature, including in soil, water, and the gastrointestinal tracts of animals and humans. Many species of Clostridium are anaerobic, meaning they can grow and reproduce in environments with little or no oxygen. Some species of Clostridium are capable of producing toxins that can cause serious and sometimes life-threatening illnesses in humans and animals.

Some notable species of Clostridium include:

* Clostridium tetani, which causes tetanus (also known as lockjaw)
* Clostridium botulinum, which produces botulinum toxin, the most potent neurotoxin known and the cause of botulism
* Clostridium difficile, which can cause severe diarrhea and colitis, particularly in people who have recently taken antibiotics
* Clostridium perfringens, which can cause food poisoning and gas gangrene.

It is important to note that not all species of Clostridium are harmful, and some are even beneficial, such as those used in the production of certain fermented foods like sauerkraut and natto. However, due to their ability to produce toxins and cause illness, it is important to handle and dispose of materials contaminated with Clostridium species carefully, especially in healthcare settings.

According to the US National Library of Medicine's Medical Subject Headings (MeSH), Succinate-CoA Ligases are defined as:

Enzymes that catalyze the conversion of succinyl-CoA and diphosphate into CoA, carbon dioxide, and a high-energy phosphate bond in an ATP or a GTP molecule. They are classified into two types according to the type of high-energy phosphate bond they form: adenosine triphosphatases (succinate-coa ligase (adenosine triphosphate)) or guanosine triphosphatases (succinate-coa ligase (guanosine triphosphate)).

Source: National Library of Medicine. (2021). Succinate-CoA Ligases. In: MeSH Database. Bethesda, MD: National Library of Medicine. Available at:

"Malonates" is not a recognized medical term. However, in chemistry, malonates refer to salts or esters of malonic acid, a dicarboxylic acid with the formula CH2(COOH)2. Malonic acid and its derivatives have been used in the synthesis of various pharmaceuticals and chemicals, but they are not typically associated with any specific medical condition or treatment. If you have encountered the term "malonates" in a medical context, it may be helpful to provide more information or seek clarification from the source.

Unsaturated fatty acids are a type of fatty acid that contain one or more double bonds in their carbon chain. These double bonds can be either cis or trans configurations, although the cis configuration is more common in nature. The presence of these double bonds makes unsaturated fatty acids more liquid at room temperature and less prone to spoilage than saturated fatty acids, which do not have any double bonds.

Unsaturated fatty acids can be further classified into two main categories: monounsaturated fatty acids (MUFAs) and polyunsaturated fatty acids (PUFAs). MUFAs contain one double bond in their carbon chain, while PUFAs contain two or more.

Examples of unsaturated fatty acids include oleic acid (a MUFA found in olive oil), linoleic acid (a PUFA found in vegetable oils), and alpha-linolenic acid (an omega-3 PUFA found in flaxseed and fish). Unsaturated fatty acids are essential nutrients for the human body, as they play important roles in various physiological processes such as membrane structure, inflammation, and blood clotting. It is recommended to consume a balanced diet that includes both MUFAs and PUFAs to maintain good health.

Acetyl-CoA C-acetyltransferase (also known as acetoacetyl-CoA thiolase or just thiolase) is an enzyme involved in the metabolism of fatty acids and ketone bodies. Specifically, it catalyzes the reaction that converts two molecules of acetyl-CoA into acetoacetyl-CoA, which is a key step in the breakdown of fatty acids through beta-oxidation.

The enzyme works by bringing together two acetyl-CoA molecules and removing a coenzyme A (CoA) group from one of them, forming a carbon-carbon bond between the two molecules to create acetoacetyl-CoA. This reaction is reversible, meaning that the enzyme can also catalyze the breakdown of acetoacetyl-CoA into two molecules of acetyl-CoA.

There are several different isoforms of Acetyl-CoA C-acetyltransferase found in various tissues throughout the body, with differing roles and regulation. For example, one isoform is highly expressed in the liver and plays a key role in ketone body metabolism, while another isoform is found in mitochondria and is involved in fatty acid synthesis.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Propionates, in a medical context, most commonly refer to a group of medications that are used as topical creams or gels to treat fungal infections of the skin. Propionic acid and its salts, such as propionate, are the active ingredients in these medications. They work by inhibiting the growth of fungi, which causes the infection. Common examples of propionate-containing medications include creams used to treat athlete's foot, ringworm, and jock itch.

It is important to note that there are many different types of medications and compounds that contain the word "propionate" in their name, as it refers to a specific chemical structure. However, in a medical context, it most commonly refers to antifungal creams or gels.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

Propylene glycol is not a medical term, but rather a chemical compound. However, it does have various applications in the medical field. Medically, propylene glycol can be used as a:

1. Vehicle for intravenous (IV) medications: Propylene glycol helps dissolve drugs that are not water-soluble and allows them to be administered intravenously. It is used in the preparation of some IV medications, including certain antibiotics, antivirals, and chemotherapeutic agents.
2. Preservative: Propylene glycol acts as a preservative in various medical products, such as topical ointments, eye drops, and injectable solutions, to prevent bacterial growth and increase shelf life.
3. Humectant: In some medical devices and pharmaceutical formulations, propylene glycol is used as a humectant, which means it helps maintain moisture and prevent dryness in the skin or mucous membranes.

The chemical definition of propylene glycol (C3H8O2) is:

A colorless, nearly odorless, viscous liquid belonging to the alcohol family. It is a diol, meaning it contains two hydroxyl groups (-OH), and its molecular formula is C3H8O2. Propylene glycol is miscible with water and most organic solvents and has applications in various industries, including pharmaceuticals, food processing, cosmetics, and industrial manufacturing.

I apologize for the confusion, but "Xanthobacter" is not a medical term or concept. It is actually a genus name in the family of bacteria known as Xanthobacteraceae. These are aerobic, gram-negative bacteria that can be found in various environments such as soil and water. They have the ability to fix nitrogen and degrade certain organic compounds, making them important members of soil microbial communities. If you have any questions related to medical terminology or concepts, I would be happy to help.

Acetyl-CoA carboxylase (ACCA) is a biotin-dependent enzyme that plays a crucial role in fatty acid synthesis. It catalyzes the conversion of acetyl-CoA to malonyl-CoA, which is the first and rate-limiting step in the synthesis of long-chain fatty acids. The reaction catalyzed by ACCA is as follows:

acetyl-CoA + HCO3- + ATP + 2H+ --> malonyl-CoA + CoA + ADP + Pi + 2H2O

ACCA exists in two isoforms, a cytosolic form (ACC1) and a mitochondrial form (ACC2). ACC1 is primarily involved in fatty acid synthesis, while ACC2 is responsible for the regulation of fatty acid oxidation. The activity of ACCA is regulated by several factors, including phosphorylation/dephosphorylation, allosteric regulation, and transcriptional regulation. Dysregulation of ACCA has been implicated in various metabolic disorders, such as obesity, insulin resistance, and non-alcoholic fatty liver disease.

Methanobacteriaceae is a family of archaea within the order Methanobacteriales. These are obligate anaerobes that obtain energy for growth by reducing carbon dioxide to methane, a process called methanogenesis. They are commonly found in anaerobic environments such as wetlands, digestive tracts of animals, and sewage sludge. Some species are thermophilic, meaning they prefer higher temperatures, while others are mesophilic, growing best at moderate temperatures. Methanobacteriaceae are important contributors to the global carbon cycle and have potential applications in bioremediation and bioenergy production.

Heptanoic acid, also known as enanthic acid, is an organic compound with the formula CH3(CH2)5COOH. It is a fatty acid with a 7-carbon chain, and it is a colorless liquid that is slightly soluble in water and fully miscible with ether and ethanol.

Heptanoic acid is not typically considered a medical term, as it is not a substance that is directly related to human health or disease. However, like other fatty acids, heptanoic acid can be metabolized in the body for energy and used in various physiological processes. Abnormal levels of certain fatty acids, including heptanoic acid, may be associated with various medical conditions, such as metabolic disorders or genetic diseases that affect fatty acid metabolism.

It's important to note that Heptanoic Acid is not a common term in medicine, and it's more related to chemistry and biochemistry fields.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Flavin Mononucleotide (FMN) is a coenzyme that plays a crucial role in biological oxidation-reduction reactions. It is derived from the vitamin riboflavin (also known as vitamin B2) and is composed of a flavin molecule bonded to a nucleotide. FMN functions as an electron carrier, accepting and donating electrons in various metabolic pathways, including the citric acid cycle and the electron transport chain, which are essential for energy production in cells. It also participates in the detoxification of harmful substances and contributes to the maintenance of cellular redox homeostasis. FMN can exist in two forms: the oxidized form (FMN) and the reduced form (FMNH2), depending on its involvement in redox reactions.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

Acetyl-CoA C-acyltransferase is also known as acyl-CoA synthetase or thiokinase. It is an enzyme that plays a crucial role in the metabolism of fatty acids. Specifically, it catalyzes the formation of an acyl-CoA molecule from a free fatty acid and coenzyme A (CoA).

The reaction catalyzed by Acetyl-CoA C-acyltransferase is as follows:

R-COOH + CoA-SH + ATP → R-CO-SCoA + AMP + PPi

where R-COOH represents a free fatty acid, and R-CO-SCoA is an acyl-CoA molecule.

This enzyme exists in several forms, each specific to different types of fatty acids. Acetyl-CoA C-acyltransferase is essential for the metabolism of fatty acids because it activates them for further breakdown in the cell through a process called beta-oxidation. This enzyme is found in various tissues, including the liver, muscle, and adipose tissue.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

Lipid A is the biologically active component of lipopolysaccharides (LPS), which are found in the outer membrane of Gram-negative bacteria. It is responsible for the endotoxic activity of LPS and plays a crucial role in the pathogenesis of gram-negative bacterial infections. Lipid A is a glycophosphatidylinositol (GPI) anchor, consisting of a glucosamine disaccharide backbone with multiple fatty acid chains and phosphate groups attached to it. It can induce the release of proinflammatory cytokines, fever, and other symptoms associated with sepsis when introduced into the bloodstream.

Intramolecular transferases are a specific class of enzymes that catalyze the transfer of a functional group from one part of a molecule to another within the same molecule. These enzymes play a crucial role in various biochemical reactions, including the modification of complex carbohydrates, lipids, and nucleic acids. By facilitating intramolecular transfers, these enzymes help regulate cellular processes, signaling pathways, and metabolic functions.

The systematic name for this class of enzymes is: [donor group]-transferring intramolecular transferases. The classification system developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) categorizes them under EC 2.5. This category includes enzymes that transfer alkyl or aryl groups, other than methyl groups; methyl groups; hydroxylyl groups, including glycosyl groups; and various other specific functional groups.

Examples of intramolecular transferases include:

1. Protein kinases (EC 2.7.11): Enzymes that catalyze the transfer of a phosphate group from ATP to a specific amino acid residue within a protein, thereby regulating protein function and cellular signaling pathways.
2. Glycosyltransferases (EC 2.4): Enzymes that facilitate the transfer of glycosyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, playing a role in the biosynthesis and modification of complex carbohydrates.
3. Methyltransferases (EC 2.1): Enzymes that transfer methyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, contributing to the regulation of gene expression and other cellular processes.

Understanding the function and regulation of intramolecular transferases is essential for elucidating their roles in various biological processes and developing targeted therapeutic strategies for diseases associated with dysregulation of these enzymes.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

Enzymes are complex protein molecules that speed up chemical reactions in the body by lowering the activation energy required for the reaction to occur. They act as catalysts, binding to specific substrates (the molecules upon which the enzyme acts) and converting them into products. Enzymes are highly specific, with most only catalyzing one type of reaction with one type of substrate.

Coenzymes are small organic molecules that assist in the catalytic function of enzymes. They often act as carriers of chemical groups or electrons during enzymatic reactions. Coenzymes bind temporarily to the enzyme, forming an active complex that can perform the biochemical reaction. After the reaction is complete, the coenzyme is released and may be reused in another reaction. Many coenzymes are vitamins or derivatives of vitamins.

Together, enzymes and coenzymes form a dynamic partnership that enables the intricate biochemical processes within living organisms to occur efficiently and effectively.

I'm sorry for any confusion, but "Hydro-Lyases" is not a recognized medical term or category in biochemistry. It seems like there might be a misunderstanding or a typo in the term.

In biochemistry, "lyases" are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis or oxidation, often forming a double bond or a ring-forming reaction. They are classified and named based on the type of bond they break.

If you meant to ask about a specific enzyme or reaction, could you please provide more context or clarify the term? I'd be happy to help further with accurate information.

Succinates, in a medical context, most commonly refer to the salts or esters of succinic acid. Succinic acid is a dicarboxylic acid that is involved in the Krebs cycle, which is a key metabolic pathway in cells that generates energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins.

Succinates can also be used as a buffer in medical solutions and as a pharmaceutical intermediate in the synthesis of various drugs. In some cases, succinate may be used as a nutritional supplement or as a component of parenteral nutrition formulations to provide energy and help maintain acid-base balance in patients who are unable to eat normally.

It's worth noting that there is also a condition called "succinic semialdehyde dehydrogenase deficiency" which is a genetic disorder that affects the metabolism of the amino acid gamma-aminobutyric acid (GABA). This condition can lead to an accumulation of succinic semialdehyde and other metabolic byproducts, which can cause neurological symptoms such as developmental delay, hypotonia, and seizures.

Parabens are a group of synthetic preservatives that have been widely used in the cosmetics and personal care product industry since the 1920s. They are effective at inhibiting the growth of bacteria, yeasts, and molds, which helps to prolong the shelf life of these products. Parabens are commonly found in shampoos, conditioners, lotions, creams, deodorants, and other personal care items.

The most commonly used parabens include methylparaben, ethylparaben, propylparaben, and butylparaben. These compounds are often used in combination to provide broad-spectrum protection against microbial growth. Parabens work by penetrating the cell wall of microorganisms and disrupting their metabolism, which prevents them from multiplying.

Parabens have been approved for use as preservatives in cosmetics and personal care products by regulatory agencies around the world, including the U.S. Food and Drug Administration (FDA) and the European Commission's Scientific Committee on Consumer Safety (SCCS). However, there has been some controversy surrounding their safety, with concerns raised about their potential to mimic the hormone estrogen in the body and disrupt normal endocrine function.

While some studies have suggested that parabens may be associated with health problems such as breast cancer and reproductive toxicity, the evidence is not conclusive, and more research is needed to fully understand their potential risks. In response to these concerns, many manufacturers have begun to remove parabens from their products or offer paraben-free alternatives. It's important to note that while avoiding parabens may be a personal preference for some individuals, there is currently no scientific consensus on the need to avoid them entirely.

Methanol, also known as methyl alcohol or wood alcohol, is a volatile, colorless, flammable liquid with a distinctive odor similar to that of ethanol (drinking alcohol). It is used in various industrial applications such as the production of formaldehyde, acetic acid, and other chemicals. In the medical field, methanol is considered a toxic alcohol that can cause severe intoxication and metabolic disturbances when ingested or improperly consumed. Methanol poisoning can lead to neurological symptoms, blindness, and even death if not treated promptly and effectively.

Glycerophosphates are esters of glycerol and phosphoric acid. In the context of biochemistry and medicine, glycerophosphates often refer to glycerol 3-phosphate (also known as glyceraldehyde 3-phosphate or glycerone phosphate) and its derivatives.

Glycerol 3-phosphate plays a crucial role in cellular metabolism, particularly in the process of energy production and storage. It is an important intermediate in both glycolysis (the breakdown of glucose to produce energy) and gluconeogenesis (the synthesis of glucose from non-carbohydrate precursors).

In addition, glycerophosphates are also involved in the formation of phospholipids, a major component of cell membranes. The esterification of glycerol 3-phosphate with fatty acids leads to the synthesis of phosphatidic acid, which is a key intermediate in the biosynthesis of other phospholipids.

Abnormalities in glycerophosphate metabolism have been implicated in various diseases, including metabolic disorders and neurological conditions.

Dimethylamine is an organic compound with the formula (CH3)2NH. It is a colorless gas that is highly soluble in water and polar solvents. Dimethylamine is a derivative of ammonia (NH3) in which two hydrogen atoms are replaced by methyl groups (CH3).

Dimethylamines, in medical terminology, typically refer to compounds that contain the functional group -N(CH3)2. These compounds can have various biological activities and may be used as drugs or therapeutic agents. For example, dimethylamine is a metabolite of choline, a nutrient important for brain function.

However, it's worth noting that "dimethylamines" is not typically used as a medical term to describe a specific condition or diagnosis. If you have any concerns about exposure to dimethylamine or its potential health effects, it would be best to consult with a healthcare professional.

Polyketide synthases (PKSs) are a type of large, multifunctional enzymes found in bacteria, fungi, and other organisms. They play a crucial role in the biosynthesis of polyketides, which are a diverse group of natural products with various biological activities, including antibiotic, antifungal, anticancer, and immunosuppressant properties.

PKSs are responsible for the assembly of polyketide chains by repetitively adding two-carbon units derived from acetyl-CoA or other extender units to a growing chain. The PKS enzymes can be classified into three types based on their domain organization and mechanism of action: type I, type II, and type III PKSs.

Type I PKSs are large, modular enzymes that contain multiple domains responsible for different steps in the polyketide biosynthesis process. These include acyltransferase (AT) domains that load extender units onto the PKS, acyl carrier proteins (ACPs) that tether the growing chain to the PKS, and ketosynthase (KS) domains that catalyze the condensation of the extender unit with the growing chain.

Type II PKSs are simpler enzymes that consist of several separate proteins that work together in a complex to synthesize polyketides. These include ketosynthase, acyltransferase, and acyl carrier protein domains, as well as other domains responsible for reducing or modifying the polyketide chain.

Type III PKSs are the simplest of the three types and consist of a single catalytic domain that is responsible for both loading extender units and catalyzing their condensation with the growing chain. These enzymes typically synthesize shorter polyketide chains, such as those found in certain plant hormones and pigments.

Overall, PKSs are important enzymes involved in the biosynthesis of a wide range of natural products with significant medical and industrial applications.

Pterins are a group of naturally occurring pigments that are derived from purines. They are widely distributed in various organisms, including bacteria, fungi, and animals. In humans, pterins are primarily found in the eye, skin, and hair. Some pterins have been found to play important roles as cofactors in enzymatic reactions and as electron carriers in metabolic pathways.

Abnormal levels of certain pterins can be indicative of genetic disorders or other medical conditions. For example, an excess of biopterin, a type of pterin, is associated with phenylketonuria (PKU), a genetic disorder that affects the body's ability to metabolize the amino acid phenylalanine. Similarly, low levels of neopterin, another type of pterin, can be indicative of immune system dysfunction or certain types of cancer.

Medical professionals may measure pterin levels in blood, urine, or other bodily fluids to help diagnose and monitor these conditions.

Streptomyces is a genus of Gram-positive, aerobic, saprophytic bacteria that are widely distributed in soil, water, and decaying organic matter. They are known for their complex morphology, forming branching filaments called hyphae that can differentiate into long chains of spores.

Streptomyces species are particularly notable for their ability to produce a wide variety of bioactive secondary metabolites, including antibiotics, antifungals, and other therapeutic compounds. In fact, many important antibiotics such as streptomycin, neomycin, tetracycline, and erythromycin are derived from Streptomyces species.

Because of their industrial importance in the production of antibiotics and other bioactive compounds, Streptomyces have been extensively studied and are considered model organisms for the study of bacterial genetics, biochemistry, and ecology.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Archaeal proteins are proteins that are encoded by the genes found in archaea, a domain of single-celled microorganisms. These proteins are crucial for various cellular functions and structures in archaea, which are adapted to survive in extreme environments such as high temperatures, high salt concentrations, and low pH levels.

Archaeal proteins share similarities with both bacterial and eukaryotic proteins, but they also have unique features that distinguish them from each other. For example, many archaeal proteins contain unusual amino acids or modifications that are not commonly found in other organisms. Additionally, the three-dimensional structures of some archaeal proteins are distinct from their bacterial and eukaryotic counterparts.

Studying archaeal proteins is important for understanding the biology of these unique organisms and for gaining insights into the evolution of life on Earth. Furthermore, because some archaea can survive in extreme environments, their proteins may have properties that make them useful in industrial and medical applications.

Sphingomyelins are a type of sphingolipids, which are a class of lipids that contain sphingosine as a backbone. Sphingomyelins are composed of phosphocholine or phosphoethanolamine bound to the ceramide portion of the molecule through a phosphodiester linkage. They are important components of cell membranes, particularly in the myelin sheath that surrounds nerve fibers. Sphingomyelins can be hydrolyzed by the enzyme sphingomyelinase to form ceramide and phosphorylcholine or phosphorylethanolamine. Abnormalities in sphingomyelin metabolism have been implicated in several diseases, including Niemann-Pick disease, a group of inherited lipid storage disorders.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Dihydroxyacetone Phosphate (DHAP) is a 3-carbon organic compound that plays a crucial role in the metabolic pathway called glycolysis. It is an intermediate molecule formed during the conversion of glucose into pyruvate, which ultimately produces energy in the form of ATP.

In the glycolytic process, DHAP is produced from glyceraldehyde 3-phosphate (G3P) in a reaction catalyzed by the enzyme triose phosphate isomerase. Then, DHAP is converted back to G3P in a subsequent step, which prepares it for further processing in the glycolytic pathway. This reversible conversion of DHAP and G3P helps maintain the equilibrium of the glycolytic process.

Apart from its role in energy metabolism, DHAP is also involved in other biochemical processes, such as the synthesis of glucose during gluconeogenesis and the formation of lipids in the liver.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

... (SCADD) is an autosomal recessive fatty acid oxidation disorder which ... The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic ... Scholia has a topic profile for Short-chain acyl-coenzyme A dehydrogenase deficiency. (Articles with short description, Short ... Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy ( ...
Hegyi, T.; Ostfeld, B.; Gardner, K. (1992). "Medium chain acyl-coenzyme a dehydrogenase deficiency and SIDS". New Jersey ... Wilcken, B.; Hammond, J.; Silink, M. (1994-05-01). "Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase ... "Medium-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". PMID 20301597. {{cite journal}}: Cite journal requires ,journal= (help ... Medium-chain acyl-CoA dehydrogenase deficiency (MCAD deficiency or MCADD) is a disorder of fatty acid oxidation that impairs ...
... is a fatty-acid metabolism disorder which prevents the body from ... Mutations in the ACADVL gene lead to inadequate levels of an enzyme called very long-chain acyl-coenzyme A (CoA) dehydrogenase ... Episodes of very long-chain acyl-coenzyme A dehydrogenase deficiency can be triggered by periods of fasting, illness, and ... "Very Long-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". In Pagon, Roberta A.; Adam, Margaret P.; Ardinger, Holly H.; Wallace ...
A molecule of coenzyme A carrying an acyl group is also referred to as acyl-CoA. When it is not attached to an acyl group, it ... Coenzyme A is also the source of the phosphopantetheine group that is added as a prosthetic group to proteins such as acyl ... Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the ... Coenzyme A is one of five crucial coenzymes that are necessary in the reaction mechanism of the citric acid cycle. Its acetyl- ...
... (EC 1.3.8.7, fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase ... general acyl CoA dehydrogenase (ambiguous), medium-chain acyl-coenzyme A dehydrogenase, acyl-CoA:(acceptor) 2,3-oxidoreductase ... "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase ... Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. (eds.). The Enzymes. Vol. 7 (2nd ed ...
2003). "Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is induced in monocyte-derived macrophages: in vivo and in vitro ... Lin S; Lu X; Chang CC; Chang TY (2004). "Human Acyl-Coenzyme A:Cholesterol Acyltransferase Expressed in Chinese Hamster Ovary ... "Entrez Gene: SOAT2 sterol O-acyltransferase 2". Chang TY, Chang CC, Cheng D; Chang (1997). "Acyl-coenzyme A:cholesterol ... 1998). "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". J. Biol. ...
Engel, Paul C.; Massey, V. (1971). "Green butyryl-coenzyme a dehydrogenase. An enzyme-acyl-coenzyme a complex". Biochemical ...
Specificities of acyl coenzyme A:phospholipid acyltransferases". J. Biol. Chem. 240: 1905-1911. PMID 14299609. Van Den Bosch H ... The systematic name of this enzyme class is acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase. Other names in ... the two substrates of this enzyme are acyl-CoA and 2-acyl-sn-glycero-3-phosphocholine, whereas its two products are CoA and ... is an enzyme that catalyzes the chemical reaction acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine ⇌ {\displaystyle \ ...
The ACADS gene associated with short-chain acyl-coenzyme A dehydrogenase deficiency. The ACADS gene is approximately 13 kb in ... Mutations of the ACADS gene are associated with deficiency of the short-chain acyl-coenzyme A dehydrogenase protein (SCADD); ... Jethva R, Bennett MJ, Vockley J (Dec 2008). "Short-chain acyl-coenzyme A dehydrogenase deficiency". Molecular Genetics and ... Acyl-CoA dehydrogenase, C-2 to C-3 short chain is an enzyme that in humans is encoded by the ACADS gene. This gene encodes a ...
Medium chain acyl dehydrogenase deficiency Reference, Genetics Home. "LCHAD deficiency". Genetics Home Reference. Retrieved ... Mutations in the HADHA gene lead to inadequate levels of an enzyme called long-chain 3-hydroxyacyl-coenzyme A (CoA) ... Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency is a rare autosomal recessive fatty acid oxidation disorder that ...
This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product ... Mutations in the ACADVL are associated with very long-chain acyl-coenzyme A dehydrogenase deficiency. The protein encoded by ... GeneReviews/NCBI/NIH/UW entry on Very long-chain acyl-coenzyme A dehydrogenase deficiency Human ACADVL genome location and ... ACADVL is linked with very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCADD), which has many symptoms, and typically ...
... (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ... Medium-chain acyl-coenzyme A dehydrogenase deficiency can be caused by mutations in the ACADM gene. More than 54 ACADM gene ... The acyl-coenzyme A dehydrogenase for medium-chain fatty acids (ACADM) enzyme is essential for converting these particular ... GeneReviews/NIH/NCBI/UW entry on Medium-Chain Acyl-Coenzyme A Dehydrogenase Deficiency GeneCard ACADM at The GDB Human Genome ...
Evidence for acyl-Coenzyme A retinol acyltransferase activity". J. Clin. Invest. 71 (3): 747-53. doi:10.1172/JCI110822. PMC ... Evidence for a fatty acyl coenzyme A: retinol acyltransferase". J. Biol. Chem. 257 (5): 2453-9. PMID 7061433. Portal: Biology v ... In enzymology, a retinol O-fatty-acyltransferase (EC 2.3.1.76) is an enzyme that catalyzes the chemical reaction acyl-CoA + ... The systematic name of this enzyme class is acyl-CoA:retinol O-acyltransferase. Other names in common use include retinol ...
Peroxisomal acyl-coenzyme A oxidase 3 is an enzyme that in humans is encoded by the ACOX3 gene. Acyl-Coenzyme A oxidase 3 also ... "Entrez Gene: ACOX3 acyl-Coenzyme A oxidase 3, pristanoyl". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to ... ACOX1 Acyl-CoA oxidase GRCh38: Ensembl release 89: ENSG00000087008 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and ...
"Effects of the acyl coenzyme A:cholesterol acyltransferase inhibitor avasimibe on human atherosclerotic lesions". Circulation. ... "Inhibitors of acyl-CoA: cholesterol O-acyl transferase (ACAT) as hypocholesterolemic agents. CI-1011: an acyl sulfamate with ... "Acyl-Coenzyme A: Cholesterol Acyltransferase Inhibition in Cancer Treatment". Anticancer Res. 39 (7): 3385-3394. doi:10.21873/ ... "Inhibitors of acyl-CoA: cholesterol O-acyl transferase (ACAT) as hypocholesterolemic agents. 6. The first water-soluble ACAT ...
Peroxisomal acyl-coenzyme A oxidase 1 is an enzyme that in humans is encoded by the ACOX1 gene. The protein encoded by this ... "Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl". Human ACOX1 genome location and ACOX1 gene details page in the UCSC ... 1994). "Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase". Biochem. Biophys. Res. ... 1996). "Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase ...
Cytosolic acyl coenzyme A thioester hydrolase is an enzyme that in humans is encoded by the ACOT7 gene. This gene encodes a ... member of the acyl coenzyme family. The encoded protein hydrolyzes the CoA thioester of palmitoyl-CoA and other long-chain ... "Entrez Gene: ACOT7 acyl-CoA thioesterase 7". Human ACOT7 genome location and ACOT7 gene details page in the UCSC Genome Browser ... 2003). "Human brain acyl-CoA hydrolase isoforms encoded by a single gene". Biochem. Biophys. Res. Commun. 299 (1): 49-56. doi: ...
"Entrez Gene: ACOT11 acyl-CoA thioesterase 11". "Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)". Protein Data ... Acyl-coenzyme A thioesterase 11 also known as StAR-related lipid transfer protein 14 (STARD14) is an enzyme that in humans is ... Glick BS, Rothman JE (Mar 1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 ( ... Ogiwara H, Tanabe T, Nikawa J, Numa S (Aug 1978). "Inhibition of rat-liver acetyl-coenzyme-A carboxylase by palmitoyl-coenzyme ...
Stadtman ER (1952). "Acyl-coenzyme A synthesis by phosphotransacetylase and coenzyme A transphorase". Fed. Proc. 11: 291. ... Other names in common use include propionate coenzyme A-transferase, propionate-CoA:lactoyl-CoA transferase, propionyl CoA: ...
"Entrez Gene: ACBD3 acyl-Coenzyme A binding domain containing 3". "ACBD3 - Golgi resident protein GCP60 - Homo sapiens (Human ...
"Entrez Gene: ACAD9 acyl-Coenzyme A dehydrogenase family, member 9". Leslie N, Wang X, Peng Y, Valencia CA, Khuchua Z, Hata J, ... "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients". ... Acyl-CoA dehydrogenase family member 9, mitochondrial is an enzyme that in humans is encoded by the ACAD9 gene. Mitochondrial ... Oey NA, Ruiter JP, Ijlst L, Attie-Bitach T, Vekemans M, Wanders RJ, Wijburg FA (July 2006). "Acyl-CoA dehydrogenase 9 (ACAD 9) ...
Glick BS, Rothman JE (1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 (6110): ...
"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the ... "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". The Journal of ... catalyzes the formation of triglycerides from diacylglycerol and fatty acyl-CoA. The reaction catalyzed by DGAT is considered ...
... palmitoyl-coenzyme A dehydrogenase, long-chain acyl-coenzyme A dehydrogenase, long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase ... Hauge JG, Crane FL, Beinert H (April 1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. ... Hall CL, Heijkenskjöld L, Bártfai T, Ernster L, Kamin H (December 1976). "Acyl coenzyme A dehydrogenases and electron- ... Long-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC ...
I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". The Journal of Biological Chemistry. 267 (2 ... Very-long-chain acyl-CoA dehydrogenase (EC 1.3.8.9, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA: ... "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients". ... Very-long-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ...
Stöveken, T; Kalscheuer R; Malkus U; Reichelt R; Steinbüchel A. (2005). "The wax ester synthase/acyl coenzyme A:diacylglycerol ... However, when using acetyl alcohol as the acyl acceptor, AWAT1 prefers saturated acyl groups, while AWAT2 shows activity with ... "Identification of the wax ester synthase/acyl-coenzyme A: diacylglycerol acyltransferase WSD1 required for stem wax ester ... The systematic name of this enzyme class is acyl-CoA:long-chain-alcohol O-acyltransferase. Other names in common use include ...
Molecular Characterization of a Major Plastidial Acyl-Coenzyme a Synthetase from Arabidopsis". Plant Physiology. 129 (4): 1700- ...
Whitaker CH, Felice KJ, Silvers D, Wu Q (August 2015). "Fulminant lipid storage myopathy due to multiple acyl-coenzyme a ... Wen B, Li D, Li W, Zhao Y, Yan C (June 2015). "Multiple acyl-CoA dehydrogenation deficiency as decreased acyl-carnitine profile ... It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but ... This shortening of neurites can be restored by riboflavin, carnitine, or Coenzyme Q10 supplements. The encoded protein ...
Sterol O-acyltransferase (acyl-Coenzyme A: cholesterol acyltransferase) 1, also known as SOAT1, is an enzyme that in humans is ... Acyl-coenzyme A:cholesterol acyltransferase (EC 2.3.1.26) is an intracellular protein located in the endoplasmic reticulum that ... Chang TY, Chang CC, Lin S, Yu C, Li BL, Miyazaki A (June 2001). "Roles of acyl-coenzyme A:cholesterol acyltransferase-1 and -2 ... Chang CC, Noll WW, Nutile-McMenemy N, Lindsay EA, Baldini A, Chang W, Chang TY (January 1994). "Localization of acyl coenzyme A ...
Molecular characterization of a major plastidial acyl-coenzyme A synthetase from Arabidopsis". Plant Physiology. 129 (4): 1700- ... Fatty acid synthase (FAS) is a large complex of enzymes and cofactors including acyl carrier protein (ACP) which holds the acyl ...
Short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD) is an autosomal recessive fatty acid oxidation disorder which ... The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic ... Scholia has a topic profile for Short-chain acyl-coenzyme A dehydrogenase deficiency. (Articles with short description, Short ... Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy ( ...
IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal. IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain ... IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily. IPR006091 Acyl-CoA oxidase/dehydrogenase, middle ... Human Disease Modeled: short chain acyl-CoA dehydrogenase deficiency. Allelic Composition. Genetic Background. Reference. ... IPR009075 Acyl-CoA dehydrogenase/oxidase, C-terminal. ... short chain acyl-CoA dehydrogenase deficiency DOID:0080154. ...
... maintenance of acyl-CoA pools within the cell and in the protection of acyl-CoAs in the cytosol from enzymes including acyl-CoA ... Role of acyl-CoA binding protein in acyl-CoA metabolism and acyl-CoA-mediated cell signaling. J. Nutr., 130, 294S-298S (2000). ... Arabidopsis Acyl-Coenzyme A-Binding Proteins The Author: Mee-Len Chye, School of Biological Sciences, University of Hong Kong, ... The presence of a conserved acyl-CoA-binding domain in each ACBP enables it to bind acyl-CoA esters. Recombinant ACBPs have ...
Learn about Acyl-CoA Dehydrogenase at online-medical-dictionary.org ... Acyl CoA Dehydrogenase. Acyl coenzyme A Dehydrogenase. Acyl-CoA Dehydrogenase, Medium-Chain. Acyl-coenzyme A Dehydrogenase. CoA ... Dehydrogenase, Acyl-CoA. Dehydrogenase, Acyl-coenzyme A. Dehydrogenase, Fatty-acyl CoA. Dehydrogenase, Medium-Chain Acyl-CoA. ... Medium Chain Acyl CoA Dehydrogenase. Medium Chain Acyl Coenzyme A Dehydrogenase. Medium Chain Acyl-CoA Dehydrogenase. Medium- ...
Here we have shown that neurons have abundant expression and activity of the long-chain cytoplasmic acyl coenzyme A (acyl-CoA) ... Here we have shown that neurons have abundant expression and activity of the long-chain cytoplasmic acyl coenzyme A (acyl-CoA) ... Here we have shown that neurons have abundant expression and activity of the long-chain cytoplasmic acyl coenzyme A (acyl-CoA) ... Here we have shown that neurons have abundant expression and activity of the long-chain cytoplasmic acyl coenzyme A (acyl-CoA) ...
Peroxisomal acyl-CoA oxidase deficiency is a disorder that causes deterioration of nervous system functions (neurodegeneration ... Ferdinandusse S, Barker S, Lachlan K, Duran M, Waterham HR, Wanders RJ, Hammans S. Adult peroxisomal acyl-coenzyme A oxidase ... Clinical, biochemical, and mutational spectrum of peroxisomal acyl-coenzyme A oxidase deficiency. Hum Mutat. 2007 Sep;28(9):904 ... Peroxisomal acyl-CoA oxidase deficiency is caused by mutations in the ACOX1 gene, which provides instructions for making an ...
The metabolism of O-acyl-N-acylneuraminic acids. Biosynthesis of O-acylated sialic acids in bovine and equine submandibular ... acyl-CoA and CoA concentrations of 33 nmol, 65 nmol and 106 nmol/g wet tissue respectively are found in fresh bovine ... Coenzyme A ...
SLC1 and SLC4 encode partially redundant acyl-Coenzyme A 1-acylglycerol-3-phosphate O-acyltransferases of budding yeast. * ... In yeast it is generated from lyso-phosphatidic acid, which is acylated by Slc1p, a sn-2-specific, acyl-Coenzyme A-dependent 1- ... SLC4 harbors a membrane bound O-acyl transferase (MBOAT) motif, and down regulation of SLC4 strongly reduces 1-acyl-sn-glycerol ... Microsomes from slc1Δ and slc4Δ cells incubated with [¹⁴C]-oleoyl-Coenzyme A in the absence of lyso-phosphatidic acid and ...
Fragmentation of fatty acyl coenzyme A molecules: …molecule undergoes a rearrangement, forming succinyl coenzyme A, which is an ... Other articles where succinyl coenzyme A is discussed: metabolism: ... In metabolism: Fragmentation of fatty acyl coenzyme A molecules. …molecule undergoes a rearrangement, forming succinyl coenzyme ... products are carbon dioxide and succinyl coenzyme A. As was noted with reaction [37], this oxidation of α-oxoglutarate results ...
In 1983, Gregersen et al demonstrated a medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) deficiency in a patient with ... Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD) * Sections Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency ... Child Neurology: medium-chain acyl-coenzyme A dehydrogenase deficiency. Neurology. 2015 Jul 28. 85 (4):e37-40. [QxMD MEDLINE ... At least 3 separate acyl-CoA dehydrogenases are known; they are as follows:. *. Long-chain acyl-CoA dehydrogenase (Length of ...
Child Neurology: medium-chain acyl-coenzyme A dehydrogenase deficiency. Neurology. 2015 Jul 28. 85 (4):e37-40. [QxMD MEDLINE ... Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD) * Sections Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency ... encoded search term (Medium-Chain Acyl-CoA Dehydrogenase (MCAD) Deficiency (MCADD)) and Medium-Chain Acyl-CoA Dehydrogenase ( ... Medium-chain acyl-CoA dehydrogenase deficiency in children with non- ketotic hypoglycemia and low carnitine levels. Pediatr Res ...
Decanoyl coenzyme A (Decanoyl CoA) is coupled with S-adenosylmethionine (SAM) by Vibrio cholera CqsA enzyme to produce a potent ... quorum-sensing molecule, 3-aminotridec-2-en-4-one (Ea-CAI-1; Decanoyl coenzyme A is a substrate for acyltransferase; ... A Novel Acyl-CoA: Diacylglycerol Acyltransferase 1 (DGAT1) inhibitor, GSK2973980A, Inhibits Postprandial Triglycerides and ... Decanoyl coenzyme A is a substrate for acyltransferase.. It is a substrate for human liver glycine-N-acylase. ...
Heat shock protein 27 deficiency promotes ferrous ion absorption and enhances acyl-Coenzyme A synthetase long-chain family ... Acyl-CoA synthetase long-chain family member 4 (ACSL4) and lysophosphatidylcholine acyltransferase 3 (LPCAT3) participate in ... Second, FIN56 binds to the enzyme squalene synthase, which leads to the depletion of endogenous antioxidant coenzyme Q10 (COQ10 ...
Chang TY, Li BL, Chang CC, Urano Y. Acyl-coenzyme A:cholesterol acyltransferases. Am J Physiol Endocrinol Metab 2009;297(1): E1 ... Conjugated and non-conjugated octadecaenoic acids affect differently intestinal acyl coenzyme A: cholesterol acyltransferase ...
Very long-chain acyl-coenzyme A dehydrogenase deficiency]] (VLCAD). *Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase ... Short-chain acyl-coenzyme A dehydrogenase deficiency (SCAD). *Short chain L-3-hydroxyacyl-coA dehydrogenase deficiency (SCHAD) ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD). * ... Other coenzyme A enzyme defiencies *2,4 Dienoyl-CoA reductase ... Before the fatty acids can be degraded, they must be converted to acyl CoA (a step called activation) and moved from the ...
Which coenzyme activates organic acids?. Definition. CoEnzyme A CoA.. soluble carrier of acyl groups. ... How do coenzymes interact with enzymes?. Definition. Via non-covalent linkages.. They operate as substrate in two-substrate ... What are the coenzymes of dehydrogenase reactions?. Definition. NAD and NADP. acquire two electrons and a proton during ...
ACAT; acyl coenzyme A:cholesterol acyltransferase; Acyl-coenzyme A:cholesterol acyltransferase; Brain carboxylesterase hBr1; ...
COENZYME A. C21 H36 N7 O16 P3 S. RGJOEKWQDUBAIZ-IBOSZNHHSA-N. Ligand Interaction. ... Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid ... Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid ... The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from ...
Name: acyl-Coenzyme A dehydrogenase, short chain. Synonyms: SCAD, Bcd-1, Bcd1, Hdlq8 ...
gi,115570,sp,P11356,CAO4_CANTR Acyl-coenzyme A oxidase PXP-2 (Acyl-CoA oxidase) gi,66056,pir,,OXCKP2 acyl-CoA oxidase.... ... gi,17373023,sp,P06598,CAO2_CANTR Acyl-coenzyme A oxidase II (Acyl-CoA oxidase) (PXP-4) (Peroxisomal fatty acyl-CoA ox.... ... gi,17373073,sp,P08790,CAO1_CANTR Acyl-coenzyme A oxidase I (Acyl-CoA oxidase) (PXP-5) gi,7548394,gb,AAA34363.2, acyl-.... ... gi,30089972,ref,NP_004026.2, acyl-Coenzyme A oxidase isoform a; acyl-coenzyme A oxidase 1 [Homo sapiens]. ...
Name: acyl-Coenzyme A oxidase 3, pristanoyl. Synonyms: EST-s59, PCOX, pristanoyl-CoA oxidase ...
Short-chain acyl-coenzyme A dehydrogenase deficiency. Mol Genet Metab. 2008 Dec; 95(4):195-200. ... Measurement of tissue acyl-CoAs using flow-injection tandem mass spectrometry: acyl-CoA profiles in short-chain fatty acid ... "Acyl-CoA Dehydrogenases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Short-chain acyl-CoA dehydrogenase deficiency: a cause of ophthalmoplegia and multicore myopathy. Neurology. 1999 Jan 15; 52(2 ...
Deficiency of medium-chain acyl-CoA dehydrogenase is a frequent and treatable metabolic defect, which can be diagnosed by ... method for the detection of phenylpropionylglycine in urine as a diagnostic tool in inherited medium-chain acyl-coenzyme A ... Deficiency of medium-chain acyl-CoA dehydrogenase is a frequent and treatable metabolic defect, which can be diagnosed by ... acid load by ion-exclusion chromatography is a rapid and reliable diagnostic tool for the detection of medium-chain acyl-CoA ...
Acyl Coenzyme A Desaturase, Cocos Nucifera (Coconut"> Milk, Squalane (Olive derived">, Ulmus Fulva (Slippery Elm"> Bark Extract ... Acyl Coenzyme A Desaturase, Persea Gratissima (Avocado"> Fruit Extract, Honey Extract, Panthenol (Provitamin B5″>, Glycine Soja ... Acyl Coenzyme A Desaturase, Glyceryl Stearate, Capric/Caprylic Triglycerides (Coconut derived">, Prunus Armeniaca (Apricot"> ... Acyl Coenzyme A Desaturase, Cetrimonium Chloride, Hydroxyethyl Cellulose, Cocos Nucifera (Coconut"> Water, Vitis Vinifera ( ...
... fatty acid coenzyme A ligase 5; fatty-acid-Coenzyme A ligase, long-chain 5; HGNC:16526; LACS 5; Long-chain acyl-CoA synthetase ... The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in ... long-chain fatty acid metabolic process long-chain fatty-acyl-CoA biosynthetic process ... Protein Aliases: Arachidonate--CoA ligase; FACL5 for fatty acid coenzyme A ligase 5; ...
... and coenzyme Q10. Administration of ketone bodies was described as a promising adjunct, but has only been documented once. We ... Multiple acyl-CoA dehydrogenase deficiency- (MADD-), also called glutaric aciduria type 2, associated leukodystrophy may be ... Multiple acyl-CoA dehydrogenase deficiency (MADD), also called glutaric aciduria type II (OMIM #231680) is a genetic defect of ... Oral sodium 3-hydroxybutyrate, a novel adjunct to treatment for multiple acyl CoA dehydrogenase deficiency. J Inherit Metab Dis ...
7. Acyl-coenzyme A thioesterase 12. General function:. Lipid transport and metabolism. Specific function:. Hydrolyzes acetyl- ... Oleoyl-[acyl-carrier-protein] + Water → [acyl-carrier-protein] + Oleic acid. details. Hexadecanoyl-[acp] + Water → Acyl-carrier ... Acetyl-CoA + Water + Oxalacetic acid → Citric acid + Coenzyme A. details. Citric acid + Coenzyme A → Acetyl-CoA + Water + ... 3R)-3-Hydroxybutanoyl-[acyl-carrier protein] → But-2-enoyl-[acyl-carrier protein] + Water. details. ...
stearoyl-CoA desaturase 1 (SCD-1); Acetyl-coenzyme carboxylase; acyl-CoA carboxylase inhibitor (ACC inhibitor); stearoyl ... 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) inhibitor; Decreases intestinal cholesterol absorption; FXR agonist; ACC ... Coenzyme A desaturase inhibitor (SCD inhibitor); THR-beta selective agonist; DGAT2 inhibitor; FASN inhibitor Aramchol; ...
  • Peroxisomal acyl-CoA oxidase deficiency is a disorder that causes deterioration of nervous system functions (neurodegeneration) beginning in infancy. (medlineplus.gov)
  • Newborns with peroxisomal acyl-CoA oxidase deficiency have weak muscle tone (hypotonia) and seizures. (medlineplus.gov)
  • Most babies with peroxisomal acyl-CoA oxidase deficiency learn to walk and begin speaking, but they experience a gradual loss of these skills (developmental regression), usually beginning between the ages of 1 and 3. (medlineplus.gov)
  • Most children with peroxisomal acyl-CoA oxidase deficiency do not survive past early childhood. (medlineplus.gov)
  • Peroxisomal acyl-CoA oxidase deficiency is a rare disorder. (medlineplus.gov)
  • Peroxisomal acyl-CoA oxidase deficiency is caused by mutations in the ACOX1 gene, which provides instructions for making an enzyme called peroxisomal straight-chain acyl-CoA oxidase. (medlineplus.gov)
  • The peroxisomal straight-chain acyl-CoA oxidase enzyme plays a role in the breakdown of certain fat molecules called very long-chain fatty acids (VLCFAs). (medlineplus.gov)
  • ACOX1 gene mutations prevent the peroxisomal straight-chain acyl-CoA oxidase enzyme from breaking down VLCFAs efficiently. (medlineplus.gov)
  • It is unclear exactly how VLCFA accumulation leads to the specific features of peroxisomal acyl-CoA oxidase deficiency. (medlineplus.gov)
  • Leukodystrophy is likely involved in the development of the neurological abnormalities that occur in peroxisomal acyl-CoA oxidase deficiency. (medlineplus.gov)
  • CAO1_RAT Acyl-coenzyme A oxidase. (cornell.edu)
  • Acyl-coenzyme A oxidase consists of three domains. (embl.de)
  • Catalase, fatty-acyl-coenzyme-A-oxidase (FAO), and total peroxisomal beta oxidation activities were determined. (cdc.gov)
  • Short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD) is an autosomal recessive fatty acid oxidation disorder which affects enzymes required to break down a certain group of fats called short chain fatty acids. (wikipedia.org)
  • medical citation needed] Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy (lethargy), poor feeding, and failure to gain weight and grow. (wikipedia.org)
  • The symptoms of short-chain acyl-CoA dehydrogenase deficiency may be triggered during illnesses such as viral infections. (wikipedia.org)
  • The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic testing Urine test The differential diagnosis for short-chain acyl-coenzyme A dehydrogenase deficiency is: ethylmalonic encephalopathy, mitochondrial respiratory chain defects and multiple acyl-CoA dehydrogenase deficiency. (wikipedia.org)
  • In terms of treatment for this condition, short-chain acyl-CoA dehydrogenase deficiency, some individuals may not need treatment, while others might follow administration of: Riboflavin Dextrose Anticonvulsants This disorder, epidemiologically speaking, is thought to affect approximately 1 in 50,000 newborns according to Jethva, et al. (wikipedia.org)
  • Scholia has a topic profile for Short-chain acyl-coenzyme A dehydrogenase deficiency. (wikipedia.org)
  • Medium-chain acyl-CoA dehydrogenase deficiency in children with non- ketotic hypoglycemia and low carnitine levels. (medscape.com)
  • Population spectrum of ACADM genotypes correlated to biochemical phenotypes in newborn screening for medium-chain acyl-CoA dehydrogenase deficiency. (medscape.com)
  • Newborn screening for medium chain acyl-CoA dehydrogenase deficiency in England: prevalence, predictive value and test validity based on 1.5 million screened babies. (medscape.com)
  • Medium-chain acyl-CoA dehydrogenase deficiency in Saudi Arabia: incidence, genotype, and preventive implications. (medscape.com)
  • Newborn screening for medium-chain acyl-CoA dehydrogenase deficiency: a global perspective. (medscape.com)
  • Medium-chain acyl-coA dehydrogenase deficiency: evaluation of genotype-phenotype correlation in patients detected by newborn screening. (medscape.com)
  • Abnormal screening in a healthy infant of a mother with undiagnosed medium-chain acyl-coA dehydrogenase deficiency. (medscape.com)
  • Child Neurology: medium-chain acyl-coenzyme A dehydrogenase deficiency. (medscape.com)
  • Newborn screening for medium-chain acyl-CoA dehydrogenase deficiency: regional experience and high incidence of carnitine deficiency. (medscape.com)
  • Medium-chain acyl-CoA dehydrogenase deficiency: genotype-biochemical phenotype correlations. (medscape.com)
  • Coordinated and reversible reduction of enzymes involved in terminal oxidative metabolism in skeletal muscle mitochondria from a riboflavin-responsive, multiple acyl-CoA dehydrogenase deficiency patient. (harvard.edu)
  • Anesthetic considerations for a patient with compound heterozygous medium-chain Acyl-CoA dehydrogenase deficiency. (harvard.edu)
  • Neonatal screening for medium--chain acyl-CoA dehydrogenase deficiency. (harvard.edu)
  • Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. (harvard.edu)
  • Short-chain acyl-CoA dehydrogenase deficiency: a cause of ophthalmoplegia and multicore myopathy. (harvard.edu)
  • We conclude that, even in asymptomatic patients, determination of phenylpropionylglycine in urine after a phenylpropionic acid load by ion-exclusion chromatography is a rapid and reliable diagnostic tool for the detection of medium-chain acyl-CoA dehydrogenase deficiency. (nih.gov)
  • Multiple acyl-CoA dehydrogenase deficiency- (MADD-), also called glutaric aciduria type 2, associated leukodystrophy may be severe and progressive despite conventional treatment with protein- and fat-restricted diet, carnitine, riboflavin, and coenzyme Q10. (nature.com)
  • The new diseases are homocystinuria, maple syrup urine disease, tyrosinemia type 1, isovaleric acidemia, glutaric aciduria type I, long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency, and carnitine deficiency. (medscape.com)
  • The presence of a conserved acyl-CoA-binding domain in each ACBP enables it to bind acyl-CoA esters. (aocs.org)
  • Recombinant ACBPs have been tested and shown to bind acyl-CoA esters in vitro using binding assays such as the Lipidex assay. (aocs.org)
  • Given that recombinant Arabidopsis ACBPs show preferences for different acyl-CoA esters and phospholipids in in vitro binding assays, it was hypothesized that members in the Arabidopsis ACBP family have nonoverlapping functions in the plant cell. (aocs.org)
  • Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. (thermofisher.com)
  • Regulation of the intramitochondrial free CoA also is affected, with accumulation of acyl-CoA esters in the mitochondria. (medscape.com)
  • The amino acid carnitine is required for the transport of long-chain fatty acyl coenzyme A (CoA) esters into myocyte mitochondria, where they are oxidized for energy. (msdmanuals.com)
  • In 1983, Gregersen et al demonstrated a medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) deficiency in a patient with hypoketotic hypoglycemia. (medscape.com)
  • Risk stratification by residual enzyme activity after newborn screening for medium-chain acyl-CoA dehyrogenase deficiency: data from a cohort study. (medscape.com)
  • Deficiency of medium-chain acyl-CoA dehydrogenase is a frequent and treatable metabolic defect, which can be diagnosed by detection of phenylpropionylglycine in urine after an oral load of phenylpropionic acid. (nih.gov)
  • Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients. (wikigenes.org)
  • For 60 years, newborn screening has tested for phenylketonuria, congenital hypothyroidism , congenital adrenal hyperplasia, sickle cell disease , cystic fibrosis and medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency. (medscape.com)
  • This acyl-CoA is linked to carnitine by the action of CPT I, with simultaneous transport across the mitochondrial membrane barrier. (medscape.com)
  • Impact of short- and medium-chain organic acids, acylcarnitines, and acyl-CoAs on mitochondrial energy metabolism. (medscape.com)
  • Brain tissue ATP concentrations, acyl-Coenzyme A thioesters, and mitochondrial content were also measured. (lu.se)
  • Acyl-CoA synthetase family member 3, mitochondrial (EC 6.2.1. (joplink.net)
  • Once inside the mitochondrion, the action of CPT II at the inner surface of the membrane releases free carnitine, which exits to the cytosol and leaves behind the acyl-CoA molecule. (medscape.com)
  • Carnitine binds acyl residues and helps in their elimination, decreasing the number of acyl residues conjugated with coenzyme A (CoA) and increasing the ratio between free and acylated CoA. (medscape.com)
  • Early investigations were focused on the 10-kDa ACBPs from mammals and yeast, and from these studies the 10-kDa ACBP has been implicated in biological roles ranging from acyl-CoA transport, maintenance of acyl-CoA pools within the cell and in the protection of acyl-CoAs in the cytosol from enzymes including acyl-CoA hydrolase, acetyl-CoA carboxylase and acyl-CoA synthetase [reviewed in 3]. (aocs.org)
  • How do coenzymes interact with enzymes? (flashcardmachine.com)
  • Acyl-CoA Dehydrogenases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Acyl-CoA Dehydrogenases" by people in Harvard Catalyst Profiles by year, and whether "Acyl-CoA Dehydrogenases" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Acyl-CoA Dehydrogenases" by people in Profiles. (harvard.edu)
  • In the cytosol, a saturated, straight-chain fatty acid molecule with no double bonds is activated by the action of fatty acyl-CoA synthetase to form its corresponding acyl-CoA. (medscape.com)
  • C6-C10-dicarboxylic aciduria: investigations of a patient with riboflavin responsive multiple acyl-CoA dehydrogenation defects. (medscape.com)
  • Entry into the beta-oxidation cycle requires the action of acyl-CoA dehydrogenase, the first enzyme in the sequence, which removes electrons from the alpha-carbon and the beta-carbon, introducing a double bond. (medscape.com)
  • Decanoyl coenzyme A (Decanoyl CoA) is coupled with S-adenosylmethionine (SAM) by Vibrio cholera CqsA enzyme to produce a potent quorum-sensing molecule, 3-aminotridec-2-en-4-one (Ea-CAI-1. (sigmaaldrich.com)
  • An enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein] in the fatty acid biosynthesis pathway. (umassmed.edu)
  • Unbiased and targeted metabolomic analysis of fasted mice with a conditional knockout of ACOT7 in the nervous system, Acot7 N-/- , revealed increased fatty acid flux into multiple long-chain acyl-CoA-dependent pathways. (johnshopkins.edu)
  • Ellis, JM , Wong, GW & Wolfgang, MJ 2013, ' Acyl coenzyme A thioesterase 7 regulates neuronal fatty acid metabolism to prevent neurotoxicity ', Molecular and cellular biology , vol. 33, no. 9, pp. 1869-1882. (johnshopkins.edu)
  • Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. (rcsb.org)
  • Measurement of tissue acyl-CoAs using flow-injection tandem mass spectrometry: acyl-CoA profiles in short-chain fatty acid oxidation defects. (harvard.edu)
  • The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. (thermofisher.com)
  • Because triglyceride is a relatively inert intracellular metabolite, it is likely that it serves more as a marker for other fatty acid-derived metabolites that actually mediate the insulin resistance, such as cytosolic long-chain acyl-CoA (LCACoA). (diabetesjournals.org)
  • molecule undergoes a rearrangement, forming succinyl coenzyme A, which is an intermediate of the TCA cycle. (britannica.com)
  • Cleavage of the 3-keto compound at the now unstable alpha-beta carbon bond and transfer of another CoA moiety to the new fragment results in 2 products: acetyl-CoA, composed of the carbonyl and original alpha-carbon from the starting molecule, and a new fatty acyl-CoA that is 2 carbons shorter than the original molecule. (medscape.com)
  • These six ACBPs map to four distinct classes based on the presence of other protein domains besides the conserved acyl-CoA-binding domain. (aocs.org)
  • This graph shows the total number of publications written about "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by people in this website by year, and whether "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" was a major or minor topic of these publications. (umassmed.edu)
  • Below are the most recent publications written about "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by people in Profiles. (umassmed.edu)
  • Pantethine helps increase the metabolic activity of Coenzyme A (CoA) and the acyl-carrier protein (ACP), which creates a reduction in cholesterol synthesis. (life-enthusiast.com)
  • Acetyl-CoA, acyl-CoA and CoA concentrations of 33 nmol, 65 nmol and 106 nmol/g wet tissue respectively are found in fresh bovine submandibular glands. (nih.gov)
  • The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. (rcsb.org)
  • These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site. (rcsb.org)
  • In plants cells, lipid-transfer proteins (LTPs) and acyl-CoA-binding proteins (ACBPs) have been identified as candidates for lipid transfer within the cell [reviewed in 1,2]. (aocs.org)
  • Here we have shown that neurons have abundant expression and activity of the long-chain cytoplasmic acyl coenzyme A (acyl-CoA) thioesterase 7 (ACOT7) to regulate lipid retention and metabolism. (johnshopkins.edu)
  • The metabolism of O-acyl-N-acylneuraminic acids. (nih.gov)
  • Mutations in the ACADS gene lead to inadequate levels of short-chain acyl-CoA dehydrogenase, which is important for breaking down short-chain fatty acids. (wikipedia.org)
  • Here we show that SLC4 (Yor175c), a gene of hitherto unknown function, encodes a second 1-acyl-sn-glycerol-3-phosphate acyltransferase. (unifr.ch)
  • The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. (rcsb.org)
  • In yeast it is generated from lyso-phosphatidic acid, which is acylated by Slc1p, a sn-2-specific, acyl-Coenzyme A-dependent 1-acylglycerol-3-phosphate O-acyltransferase. (unifr.ch)
  • SLC4 harbors a membrane bound O-acyl transferase (MBOAT) motif, and down regulation of SLC4 strongly reduces 1-acyl-sn-glycerol-3-phosphate acyltransferase activity in microsomes from slc1Δ cells. (unifr.ch)
  • Decanoyl coenzyme A is a substrate for acyltransferase. (sigmaaldrich.com)
  • The function of the acyl-CoA-binding domain in recombinant Arabidopsis ACBPs expressed in the bacterium Escherichia coli was established using site-directed mutagenesis followed by in vitro binding assays. (aocs.org)
  • ACBP3 lacks both ankyrin repeats and kelch motifs but it is larger (39.3 kDa) than ACBP6 (10.4 kDa), which is the smallest member and consists of only the acyl-CoA-binding domain. (aocs.org)
  • Any donor that can transfer acyl groups between molecular entities. (ebi.ac.uk)
  • Increases in intramyocellular long-chain fatty acyl-CoAs (LCACoA) have been implicated in the pathogenesis of insulin resistance in skeletal muscle. (diabetesjournals.org)
  • A medium-chain fatty acyl-CoA that results from the formal condensation of the thiol group of coenzyme A with the carboxy group of lauric (dodecanoic) acid. (ebi.ac.uk)
  • products are carbon dioxide and succinyl coenzyme A. As was noted with reaction [37], this oxidation of α-oxoglutarate results in the reduction of lipS 2 , which must be reoxidized. (britannica.com)
  • It has a preference for acyl derivatives with carbon chain length from 4 to 16. (umassmed.edu)
  • Finally, there was no change in acyl-coenzyme A thioesters between the two groups. (lu.se)
  • the E-value for the Acyl-CoA_ox_N domain shown below is 4.1e-30. (embl.de)