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.
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.
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.
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.
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).
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)
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.
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)
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.-.
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.
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)

Very-long-chain and branched-chain fatty acyl-CoAs are high affinity ligands for the peroxisome proliferator-activated receptor alpha (PPARalpha).: Very-long-ch
To elucidate cellular mechanisms of insulin resistance induced by excess dietary fat, we studied conscious chronically high-fat-fed (HFF) and control chow diet-fed rats during euglycemic-hyperinsulinemic (560 pmol/l plasma insulin) clamps. Compared with chow diet feeding, fat feeding significantly impaired insulin action (reduced whole body glucose disposal rate, reduced skeletal muscle glucose metabolism, and decreased insulin suppressibility of hepatic glucose production [HGP]). In HFF rats, hyperinsulinemia significantly suppressed circulating free fatty acids but not the intracellular availability of fatty acid in skeletal muscle (long chain fatty acyl-CoA esters remained at 230% above control levels). In HFF animals, acute blockade of beta-oxidation using etomoxir increased insulin-stimulated muscle glucose uptake, via a selective increase in the component directed to glycolysis, but did not reverse the defect in net glycogen synthesis or glycogen synthase. In clamp HFF animals, etomoxir did not
To elucidate cellular mechanisms of insulin resistance induced by excess dietary fat, we studied conscious chronically high-fat-fed (HFF) and control chow diet-fed rats during euglycemic-hyperinsulinemic (560 pmol/1 plasma insulin) clamps. Compared with chow diet feeding, fat feeding significantly impaired insulin action (reduced whole body glucose disposal rate, reduced skeletal muscle glucose metabolism, and decreased insulin suppressibility of hepatic glucose production [HGP]). In HFF rats, hyperinsulinemia significantly suppressed circulating free fatty acids but not the intracellular availability of fatty acid in skeletal muscle (long chain fatty acyl-CoA esters remained at 230% above control levels). In HFF animals, acute blockade of β-oxidation using etomoxir increased insulin-stimulated muscle glucose uptake, via a selective increase in the component directed to glycolysis, but did not reverse the defect in net glycogen synthesis or glycogen synthase. In clamp HFF animals, etomoxir did ...
The antidiabetic efficacy of first-line insulin sensitizers (e.g., metformin, glitazones) is accounted for by activation of AMP-activated protein kinase (AMPK). Long chain fatty acids (LCFA) activate AMPK, but their putative antidiabetic efficacy is masked by their beta-oxidized or esterified lipid …
The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. 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. This isozyme preferentially utilizes arachidonate as substrate. The absence of this enzyme may contribute to the mental retardation or Alport syndrome. Alternative splicing of this gene generates multiple transcript variants. [provided by RefSeq, Jan 2016 ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
TY - JOUR. T1 - Acyl-CoA binding protein is an essential protein in mammalian cell lines. AU - Knudsen, Jens. AU - Færgeman, Nils J.. PY - 2002/12/15. Y1 - 2002/12/15. N2 - In the present work, small interference RNA was used to knock-down acyl-CoA binding protein (ACBP) in HeLa, HepG2 and Chang cells. Transfection with ACBP-specific siRNA stopped growth, detached cells from the growth surface and blocked thymidine and acetate incorporation. The results show that depletion of ACBP in mammalian cells results in lethality, suggesting that ACBP is an essential protein.. AB - In the present work, small interference RNA was used to knock-down acyl-CoA binding protein (ACBP) in HeLa, HepG2 and Chang cells. Transfection with ACBP-specific siRNA stopped growth, detached cells from the growth surface and blocked thymidine and acetate incorporation. The results show that depletion of ACBP in mammalian cells results in lethality, suggesting that ACBP is an essential protein.. KW - Acetates. KW - ...
In the present work, small interference RNA was used to knock-down acyl-CoA binding protein (ACBP) in HeLa, HepG2 and Chang cells. Transfection with ACBP-specific siRNA stopped growth, detached cells from the growth surface and blocked thymidine and acetate incorporation. The results show that depletion of ACBP in mammalian cells results in lethality, suggesting that ACBP is an essential protein.. ...
TY - JOUR. T1 - Identification of a Mammalian Long Chain Fatty Acyl Elongase Regulated by Sterol Regulatory Element-binding Proteins. AU - Moon, Young Ah. AU - Shah, Nila A.. AU - Mohapatra, Suchismita. AU - Warrington, Janet A.. AU - Horton, Jay D.. PY - 2001/11/30. Y1 - 2001/11/30. N2 - Fatty acids are synthesized de novo from acetyl-CoA and malonyl-CoA through a series of reactions mediated by acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS). In rodents, the principal fatty acid produced by FAS is palmitic acid (16:0). Sterol regulatory element-binding proteins (SREBPs) enhance the transcription of many genes responsible for fatty acid synthesis. In transgenic mice that overexpress SREBPs in liver, the rate of fatty acid synthesis is markedly increased, owing to the activation of these biosynthetic genes, which include ATP citrate lyase, ACC, FAS, and stearoyl-CoA desaturase. The fatty acids that accumulate in livers of SREBP transgenic mice are 18 carbons rather than 16 carbons in ...
Arabidopsis acyl-CoA-binding protein ACBP6 localizes in the phloem and affects jasmonate composition.: Arabidopsis thaliana ACYL-COA-BINDING PROTEIN6 (AtACBP6)
Benzoyl-CoA is a common intermediate in the anaerobic bacterial metabolism of many aromatic substrates. Two enzymes and ferredoxin of the central benzoyl-CoA pathway in Thauera aromatica have been purified so far. Benzoyl-CoA reductase reduces the aromatic ring with reduced ferredoxin yielding cyclohexa-1,5-diene-1-carbonyl-CoA [Boll, M. & Fuchs, G. (1995) Eur. J. Biochem. 234, 921-933]. Dienoyl-CoA hydratase subsequently adds one molecule of water and thereby produces 6-hydroxycyclohex-1-ene-1-carbonyl-CoA [Laempe, D., Eisenreich, W., Bacher, A., & Fuchs, G. (1998) Eur. J. Biochem. 255, 618-627]. Here two new enzymes, which convert this intermediate to the noncyclic product 3-hydroxypimelyl-CoA, were purified from T. aromatica and studied. 6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase is an NAD(+)-specific beta-hydroxyacyl-CoA dehydrogenase that catalyzes 6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD(+) --| 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H(+). 6-Oxocyclohex-1-ene-1-carbonyl-CoA
Acyl-CoA synthetase (ACS; fatty acid:CoA ligase, AMP binding forming, EC 6.2.1.3) catalyzes the formation of acyl-CoA thioesters from free fatty acids in the presence of CoA, ATP, and Mg2+. This activation is a critical step in fatty acid metabolism in prokaryotes and eukaryotes. In fact, fatty acyl-CoAs represent important bioactive compounds, which are involved in many cellular processes in addition to serving as substrates for lipid biosynthesis and β-oxidation (Schulz, 1991).. Recent published papers have confirmed the importance of ACSs in various organisms. In Escherichia coli, ACS plays a pivotal role in the uptake of long-chain fatty acids and in regulating of the global transcriptional regulator FadR (Black et al., 1997). The E. coli ACS gene was cloned and its sequence is found to have a segment of 25 highly conserved amino acid residues that Black et al. (1997) proposed as a signature motif common to the family of fatty ACSs. In yeast (Saccharomyces cerevisiae), the activation of ...
Title: Stable isotope dilution liquid chromatography/mass spectrometry analysis of cellular and tissue medium- and long-chain acyl-coenzyme A thioesters.. Authors: Snyder, Nathaniel W; Basu, Sankha S; Zhou, Zinan; Worth, Andrew J; Blair, Ian A. Published In Rapid Commun Mass Spectrom, (2014 Aug 30). Abstract: Acyl-Coenzyme A (CoA) thioesters are the principal form of activated carboxylates in cells and tissues. They are employed as acyl carriers that facilitate the transfer of acyl groups to lipids and proteins. Quantification of medium- and long-chain acyl-CoAs represents a significant bioanalytical challenge because of their instability.Stable isotope dilution liquid chromatography/selected reaction monitoring-mass spectrometry (LC/SRM-MS) provides the most specific and sensitive method for the analysis of CoA species. However, relevant heavy isotope standards are not available and they are challenging to prepare by chemical synthesis. Stable isotope labeling by essential nutrients in cell ...
DBI - DBI (untagged)-Human diazepam binding inhibitor (GABA receptor modulator, acyl-CoA binding protein) (DBI), transcript variant 1 available for purchase from OriGene - Your Gene Company.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
cyclohexa-1,5-diene-1-carboxyl-CoA hydratase: involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica; N-terminal amino acid sequence in first source
hsa:84320 no KO assigned , (RefSeq) ACBD6; acyl-CoA binding domain containing 6 (A) MASSFLPAGAITGDSGGELSSGDDSGEVEFPHSPEIEETSCLAELFEKAAAHLQGLIQVA SREQLLYLYARYKQVKVGNCNTPKPSFFDFEGKQKWEAWKALGDSSPSQAMQEYIAVVKK LDPGWNPQIPEKKGKEANTGFGGPVISSLYHEETIREEDKNIFDYCRENNIDHITKAIKS KNVDVNVKDEEGRALLHWACDRGHKELVTVLLQHRADINCQDNEGQTALHYASACEFLDI VELLLQSGADPTLRDQDGCLPEEVTGCKTVSLVLQRHTTGKA ...
Complete information for ACBD3 gene (Protein Coding), Acyl-CoA Binding Domain Containing 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for ACBD3 gene (Protein Coding), Acyl-CoA Binding Domain Containing 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
PAC275Hu01, ACOX; PALMCOX; SCOX; Peroxisomal Acyl-Coenzyme A Oxidase 1; Straight-chain acyl-CoA oxidase | Products for research use only!
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கொழுப்பு அமிலங்கள், அல்லது கொழுப்பு அமிலத்தின் மீதங்கள் கொழுப்பு அமில தொகுப்பு எனப்படும் செயல்முறை மூலம் அசிட்டைல்- CoA உடன் மெலோனைல்-CoA அல்லது மெதில்மெலோனைல்-CoA தொகுதிகளை முன்தொடராகக் கொண்ட சங்கிலித் தொடர் நீட்சியாக்கத்தினால் கொழுப்பு அமில தொகுப்பு எனப்படும் செயல்முறை மூலம் தயாரிக்கப்பட்ட வேறுபட்ட மூலக்கூறுகளின் தொகுதியாகும்.[6][7] இவை ஐதரோகார்பன் சங்கிலி யால் ...
Other articles where Ethylmalonyl-CoA pathway is discussed: metabolism: Anaplerotic routes: …cellular building blocks include the ethylmalonyl-CoA pathway and the methylaspartate pathway. The ethylmalonyl-CoA pathway is used by organisms lacking the isocitrate lyase enzyme, such as the bacterium Rhodobacter sphaeroides. In this pathway two acetyl-CoA molecules are combined to produce acetoactyl-CoA, which subsequently reacts to form the intermediate ethylmalonyl-CoA. Ethylmalonyl-CoA is…
Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins. ...
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Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.
Fatty acyl-CoA synthetase (fatty acid: CoA ligase, AMP-forming; (EC 6.2.1.3)) catalyzes the formation of fatty acyl-CoA by a two-step process that proceeds through the hydrolysis of pyrophosphate. Fatty acyl-CoA represents bioactive compounds that are involved in protein transport, enzyme activation, protein acylation, cell signaling, and transcriptional control in addition to serving as substrates for beta oxidation and phospholipid biosynthesis. Fatty acyl-CoA synthetase occupies a pivotal role in cellular homeostasis, particularly in lipid metabolism. Our interest in fatty acyl-CoA synthetase stems from the identification of this enzyme, long-chain fatty acyl-CoA ligase (LCFA) by microarray analysis. We found this enzyme to be differentially expressed by |i|Leishmania donovani|/i| amastigotes resistant to antimonial treatment. In the present study, we confirm the presence of long-chain fatty acyl-CoA ligase gene in the genome of clinical isolates of |i|Leishmania donovani|/i| collected from the
Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent (By similarity).
An LC-MS-based method was used to determine whether platelets isolated from patients with FRDA exhibit differentiable metabolism compared with healthy controls. Isotopologue analysis showed a marked decrease in glucose incorporation with a concomitant increase in palmitate-derived acyl-CoA thioesters in FRDA platelets compared with controls. These findings demonstrate that platelets can be used as a surrogate tissue for in vivo biomarker studies to monitor new therapeutic approaches for the treatment of FRDA.. Read more: Stable isotopes and LC-MS for monitoring metabolic disturbances in Friedreichs ataxia platelets. ...
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Wax esters occur widely among bacteria, plants and mammals. Due to their special properties, they have many applications such as lubricants, cosmetics, pharmaceutical products, ink, polishes and candles. They are also considered as potential biofuels and biolubricants in the future. Wax ester producing enzymes synthesize wax esters from alcohols and fatty acyl coenzyme A thioesters. There are three gene families encoding enzymes capable of synthesizing wax esters. Two of them exist in plans; the jojoba-like wax synthase (WS), and the bifunctional wax synthase/diacylglycerol acyl transferase (WS/DGAT). We investigated the phylogenetic relationships among and between WS and WS/DGAT, based upon primary sequence homology of the encoded proteins. Nine candidate genes were chosen for experimental characterization in yeast and Arabidopsis seed. In yeast heterologous expression system, three of the expressed gene products were detected immunologically, Arabidopsis WS At5g55340, a maize WS and a moss WS.
Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA ...
Triacylglycerol (TAG) is a major component of lipid storage in yeast. The acyl CoA: diacylgycerol acyltransferase (DGAT) that catalyzes the final and rate-limiting step in the production of TAG is rather interesting. Consequently, cloning and analysis of the gene-encoding TAG synthase, diacylglycerol acyltransferase gene (DGA1), of the oleaginous yeast Rhodosporidiobolus fluvialis DMKU-RK253 were undertaken. Analysis of the deduced amino acid sequence of DGA1 from R. fluvialis DMKU-RK253 (RfDGA1) showed similarity with the acyl-CoA:diacylglycerol acyltransferase 2 (DGAT2) from other organisms. The cDNA of RfDGA1 was cloned into the yeast expression vector pYES2 and heterologously overexpressed in Saccharomyces cerevisiae. One of the transformants showed a 1.6-fold increase in lipid content compared with the wild-type strain harbouring the pYES2 empty vector. Furthermore, DGA1 overexpression in R. fluvialis DMKU-RK253 resulted in a 2.5-fold increase in lipid content when compared with the wild-type
The first committed step of fatty acid and polyketides biosynthesis, the biotin-dependent carboxylation of an acyl-CoA, is catalyzed by acyl-CoA carboxylases (ACCases) such as acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC). ACC and PCC in Streptomyces coelicolor are homologues multisubunit complexes that can carboxylate different short chain acyl-CoAs. While ACC is able to carboxylate acetyl-, propionyl-, or butyryl-CoA with approximately the same specificity, PCC only recognizes propionyl- and butyryl-CoA as substrates. How ACC and PCC have such different specificities towards these substrates is only partially understood. To further understand the molecular basis of how the active site residues can modulate the substrate recognition, we mutated D422, N80, R456 and R457 of PccB, the catalytic beta subunit of PCC. The crystal structures of six PccB mutants and the wild type crystal structure were compared systematically to establish the sequence-structure-function relationship ...
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs ...
ACSL1, CT (ACSL1, FACL1, FACL2, LACS, LACS1, LACS2, Long-chain-fatty-acid-CoA ligase 1, Acyl-CoA synthetase 1, Long-chain acyl-CoA synthetase 1, Long-chain acyl-CoA synthetase 2, Long-chain fatty acid-CoA ligase 2, Palmitoyl-CoA ligase 1, Palmitoyl-CoA ligase 2 ...
B: The influence of substrate and products on Them1 dimerization was determined by … Substrate specificities Belinostat molecular weight We next examined the thioesterase activities of Them1 and of THEM1a and THEM1b using acetyl-CoA (Fig. 3A) and palmitoyl-CoA (Fig. 3B) as substrates. Acot12, Them1, THEM1a, and THEM1b each hydrolyzed acetyl-CoA molecules, with values of Km and Vmax (Table 1) for Them1, THEM1a, and THEM1b that were each somewhat higher than for Acot12 (Km = 34.1 �� 2.1 ��M; Vmax = 57.2 �� 4.4 nmol/min/mg). As was the case for Them1, THEM1a and THEM1b exhibited robust thioesterase activity toward palmitoyl-CoA, with similar Km values for each but with Them1 exhibiting a higher value of Vmax compared with THEM1a and THEM1b (Table 1). However, as has been previously reported (18), Acot12 had no appreciable palmitoyl-CoA thioesterase activity (Fig.. 3B). Table 1 also lists for Them1 the steady-state enzymatic constants for a variety of acyl-CoA molecular species. These ...
Last updated on November 19, 2018 at 17:16. You should know the MRTs very well (use flashcards), and also know what reaction is impaired in a few diseases. You can be asked questions about the smallest things, and some questions can be so vague youre not even sure what theyre asking. You should always ask teachers to clarify questions you dont understand. However, if you know the MRTs well, and know most of whats written here, you should at least pass. In some topics, you might only need to know the summary. For each cofactor should you memorize 4 reactions that needs these cofactors. You are going to be asked about one or two diseases.. I recommend these flashcards: http://www.cram.com/flashcards/biochemistry-1-8719205. You are going to get a question about ATP calculation, like What is the ATP gain of degradation of hexanoyl-CoA to O2 and H2O?. They can ask you about degradation of fatty acids, ketone bodies or intermediates in the glycolysis or TCA. The first two are very well explained ...
H2O + hexanoyl-CoA ,=, adenosine 3,5-bisphosphate + 2 H(+) + hexanoyl-4-phosphopantetheine Last modified: 2016-05-27. Chemically balanced: yes. ...
All Pacific Roots products are tested in an independent third-party lab to confirm label accuracy. The results of a third-party labs test results are called Certificates of Analysis (COAs). Our COAs test for the potency of cannabinoids like CBD and THC. The COAs show that Pacific Roots products are at or below the legal limit of .3% THC per the 2018 Farm Bill.. Click on your product below to view the associated COA.. ...
Bacteria are the only known steroid degraders, but the pathway responsible for degrading the last two steroid rings has yet to be elucidated. In Mycobacterium tuberculosis, this pathway includes virulence determinants. Using a series of mutants in M. tuberculosis and related bacteria, we identified a number of novel CoA thioesters as pathway intermediates. Analysis of the metabolites combined with enzymological studies... ...
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Acting as the Chief Guest at the passing-out parade held at Pakistan Military Academy (PMA) in Kakul, Abbottabad, on Saturday, the Chief of the Army Staff
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Formula: C14H18N2O8MW: 342. 31CAS: 23646-68-6MDL: MFCD01457171TNP: TNP004214-NITROPHENYL PALMITATE (4-NITROPHENYL HEXADECANOATE; LogP: 2....
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TY - JOUR. T1 - Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix. AU - Wagner, Gregory R.. AU - Payne, R. Mark. PY - 2013/10/4. Y1 - 2013/10/4. N2 - Background:The mechanisms initiating protein acylation in mitochondria are unknown. Results:The pH and acyl-CoA concentrations of the mitochondrial matrix are sufficient to cause protein lysine acetylation and succinylation. Conclusion:Protein acylation in mitochondria may be a nonenzymatic event facilitated by the alkaline pH and high acyl-CoA concentrations. Significance:The mitochondrial deacylases SIRT3 and SIRT5 may have evolved to regulate nonenzymatic protein acylation.. AB - Background:The mechanisms initiating protein acylation in mitochondria are unknown. Results:The pH and acyl-CoA concentrations of the mitochondrial matrix are sufficient to cause protein lysine acetylation and succinylation. Conclusion:Protein acylation in mitochondria may be a ...
Looking for online definition of acyl coenzyme A:cholesterol acyltransferase in the Medical Dictionary? acyl coenzyme A:cholesterol acyltransferase explanation free. What is acyl coenzyme A:cholesterol acyltransferase? Meaning of acyl coenzyme A:cholesterol acyltransferase medical term. What does acyl coenzyme A:cholesterol acyltransferase mean?
Glioblastoma is the most common primary brain tumor in adults and one of its hallmarks is resistance to apoptosis. Acyl-CoA: cholesterol acyltransferase (ACAT) is an intracellular membrane-bound enzyme that uses cholesterol and long chain fatty acyl-CoA as substrates to produce cholesteryl esters. T …
Long chain fatty acid synthetases (LACSs) activate the fatty acid chains produced by plastidial de novo biosynthesis to generate acyl-CoA derivatives, important intermediates in lipid metabolism. Oilseeds, like sunflower, accumulate high levels of triacylglycerols (TAGs) in their seeds to nourish the embryo during germination. This requires that sunflower seed endosperm supports very active glycerolipid synthesis during development. Sunflower seed plastids produce large amounts of fatty acids, which must be activated through the action of LACSs, in order to be incorporated into TAGs. We cloned two different LACS genes from developing sunflower endosperm, HaLACS1 and HaLACS2, which displayed sequence homology with Arabidopsis LACS9 and LACS8 genes, respectively. These genes were expressed at high levels in developing seeds and exhibited distinct subcellular distributions. We generated constructs in which these proteins were fused to green fluorescent protein and performed transient expression ...
The elevation of synthesis and export of fatty acids from the chloroplast following N deprivation could indicate that TAG is assembled from fatty acids that are synthesized de novo. This step would require the activation of the fatty acids by a long-chain acyl-CoA synthetase. In fact, increased abundance of RNA encoding a putative long-chain acyl-CoA synthetase was observed, and the respective protein has been identified in the lipid droplet proteome (Moellering and Benning, 2010). However, another enzyme that could contribute to the changing spectrum of fatty acids is a putative phospholipid/glycerol acyltransferase, for which the transcript level decreased during N deprivation. Long-chain acyl-CoA synthetases are likely to play a key role in determining the fate of fatty acids in the cell (Shockey et al., 2002). Regulation of the respective genes could be a major factor in controlling the flux of fatty acids toward glycerolipid synthesis and their degradation by β-oxidation.. Major ...
Biotin is an essential vitamin in plants and mammals, functioning as the carbon dioxide carrier within central lipid metabolism. Bacterial pimeloyl-CoA synthetase (BioW) acts as a highly specific substrate-selection gate, ensuring the integrity of the carbon chain in biotin synthesis. BioW catalyzes the condensation of pimelic acid (C7 dicarboxylic acid) with CoASH in an ATP-dependent manner to form pimeloyl-CoA, the first dedicated biotin building block. Multiple structures of Bacillus subtilis BioW together capture all three substrates, as well as the intermediate pimeloyl-adenylate and product pyrophosphate (PPi), indicating that the enzyme uses an internal ruler to select the correct dicarboxylic acid substrate. Both the catalytic mechanism and the surprising stability of the adenylate intermediate were rationalized through site-directed mutagenesis. Building on this understanding, BioW was engineered to synthesize high-value heptanoyl (C7) and octanoyl (C8) monocarboxylic acid-CoA and C8 ...
Cellular metabolites, such as acyl-CoA, can modify proteins, leading to protein posttranslational modifications (PTMs). One such PTM is lysine succinylation, which is regulated by sirtuin 5 (SIRT5). Although numerous proteins are modified by lysine succinylation, the physiological significance of lysine succinylation and SIRT5 remains elusive. Here, by profiling acyl-CoA molecules in various mouse tissues, we have discovered that different tissues have different acyl-CoA profiles and that succinyl-CoA is the most abundant acyl-CoA molecule in the heart. This interesting observation has prompted us to examine protein lysine succinylation in different mouse tissues in the presence and absence of SIRT5. Protein lysine succinylation predominantly accumulates in the heart whenSirt5is deleted. Using proteomic studies, we have identified many cardiac proteins regulated by SIRT5. Our data suggest that ECHA, a protein involved in fatty acid oxidation, is a major enzyme that is regulated by SIRT5 and ...
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Predicted to have protein kinase A regulatory subunit binding activity. Predicted to be involved in steroid biosynthetic process. Predicted to localize to the Golgi membrane. Is expressed in brain; genitourinary system; gut; and lung. Orthologous to human ACBD3 (acyl-CoA binding domain containing 3 ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes the mitochondrial enzyme methylmalonyl Coenzyme A mutase. In humans, the product of this gene is a vitamin B12-dependent enzyme which catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, while in other species this enzyme may have different functions. Mutations in this gene may lead to various types of methylmalonic aciduria. [provided by RefSeq, Jul 2008 ...
BioAssay record AID 144067 submitted by ChEMBL: Tested for Inhibitory concentration against human N-myristoyltransferase (NMT) in radiochemical HPLC end point assay with peptide GNAASARR-NH2 and [3H]myristoyl-CoA radioligand at 1 uM; ND=Not determined.
The Chief of Army Staff(COAS) Lieutenant General Faruk Yahaya has urged officers and soldiers of the Nigerian Army (NA) to extensively deploy simulation
Mouse polyclonal Methylmalonyl Coenzyme A mutase antibody validated for WB, IHC, ICC/IF and tested in Human and Rat. Referenced in 2 publications and 1…
1NTI: Subtle structural response to ligand binding revealed by residual dipolar coupling refined NMR structures of acyl coenzyme A binding protein
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Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups ...
Atmospheric oxygen: Useful for more than just breathing.... (NB: If you attended the ENV Zuckerman Symposium last month, you will have seen the 10-minute preview version of this talk. Whether or not you were at Zuckerman, please come along for the extended version, detailing the exciting research activities that the COAS CRAM Group have been and will be getting up to). ...
Note: Direction is Device relative Bus (other Devices). All odd-numbered pins, except pin 25, are connected to ground. Pin 25 is left open. ...
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 ...
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 ...
Zabielska J, Sledzinski T, Stelmanska E (July 2019). "Acyl-Coenzyme A: Cholesterol Acyltransferase Inhibition in Cancer ... "Inhibitors of acyl-CoA: cholesterol O-acyl transferase (ACAT) as hypocholesterolemic agents. CI-1011: an acyl sulfamate with ... "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. 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 ...
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 ...
... acyl-activating enzyme, fatty acid elongate, fatty acid activating enzyme, fatty acyl coenzyme A synthetase, medium chain acyl- ... Massaro EJ; Lennarz WJ (1965). "The partial purification and characterization of a bacterial fatty acyl coenzyme A synthetase ... Glycine conjugation of mitochondrial acyl-CoAs, catalyzed by glycine N-acyltransferase (GLYAT, E.C. 2.3.1.13), is an important ... Websterlt JR, Gerowin LD, Rakita L (1965). "Purification and characteristics of a butyryl coenzyme A synthetase from bovine ...
... is part of a family known as Acyl-coenzyme A synthetases (ACSs), which catalyze the initial reaction in fatty acid ... Watkins PA, Maiguel D, Jia Z, Pevsner J (Dec 2007). "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human ... "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome". Journal of Lipid Research. 48 (12): 2736-50. ... Acyl-CoA synthetase short-chain family member 3 is a protein that in humans is encoded by the ACSS3 gene. ...
... to give a fatty acyl-adenylate, which then reacts with free coenzyme A to give a fatty acyl-CoA molecule. In order for the acyl ... Abbreviations: ACP - Acyl carrier protein, CoA - Coenzyme A, NADP - Nicotinamide adenine dinucleotide phosphate. Note that ... Acyl-carnitine is converted back to acyl-CoA by carnitine palmitoyltransferase II, located on the interior face of the inner ... Beta oxidation, in the mitochondrial matrix, then cuts the long carbon chains of the fatty acids (in the form of acyl-CoA ...
... acyl-CoA acyltransferase. This enzyme participates in ether lipid metabolism. Waku K, Lands WE (1968). "Acyl coenzyme A:1- ... In enzymology, a plasmalogen synthase (EC 2.3.1.25) is an enzyme that catalyzes the chemical reaction acyl-CoA + 1-O-alk-1-enyl ... The systematic name of this enzyme class is acyl-CoA:1-O-alk-1-enyl-glycero-3-phosphocholine 2-O-acyltransferase. Other names ... the two substrates of this enzyme are acyl-CoA and 1-O-alk-1-enyl-glycero-3-phosphocholine, whereas its two products are CoA ...
Watkins PA, Maiguel D, Jia Z, Pevsner J (December 2007). "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the ... Acyl-CoA synthetase family member 3 is an enzyme that in humans is encoded by the ACSF3 gene. The ACSF3 gene is located on the ... "Entrez Gene: Acyl-CoA synthetase family member 3". Retrieved 2011-12-30. Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, et al ... "Acyl-CoA synthetase family member 3, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).[permanent dead ...
"Acyl-coenzyme A binding protein expression alters liver fatty acyl-coenzyme A metabolism". Biochemistry. 44 (30): 10282-97. doi ... Acyl-CoA cholesterol acyl transferase EC 2.3.1.26, more simply referred to as ACAT, also known as sterol O-acyltransferase ( ... Although studies in vitro and in yeast suggest that the acyl-CoA binding protein (ACBP) may modulate long-chain fatty acyl-CoA ... Sterol O-acyltransferase (also called Acyl-CoA cholesterol acyltransferase, Acyl-CoA cholesterin acyltransferase[citation ...
"Entrez Gene: DBI diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)". Papadopoulos V, Brown ... Acyl-CoA-binding protein in humans belongs to the family of Acyl-CoA-binding proteins. This gene encodes diazepam binding ... and long-chain acyl-Coenzyme A esters. Diazepam binding inhibitor also mediates the feedback regulation of pancreatic secretion ... 1993). "Acyl-CoA-binding protein/diazepam-binding inhibitor gene and pseudogenes. A typical housekeeping gene family". J. Mol. ...
"Entrez Gene: DBI diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)". Kos M, Reid G, Denger ...
The participant coenzymes (NAD+, NADH + H+, ATP and ADP), inorganic phosphate, H2O and CO2 were omitted in these ... and into the matrix where they can either be oxidized and combined with coenzyme A to form CO2, acetyl-CoA, and NADH,[34] or ... allowing FADH2 to donate its electrons directly to coenzyme Q (ubiquinone) which is part of the electron transport chain which ...
Acyl carrier protein. *Adaptor protein. *Cholesterylester transfer protein. *F-box protein. *GTP-binding protein ...
EC 6.3.2.31 coenzyme F420-0:L-glutamate ligase EC 6.3.2.32 coenzyme γ-F420-2:α-L-glutamate ligase EC 6.3.2.33 ... acyl- carrier -proteine] ligase EC 6.2.1.21 remplacé par EC 6.2.1.30 EC 6.2.1.22 [citrate (pro-3S)-lyase] ligase EC 6.2.1.23 ... butirosin acyl-carrier protein]-L-glutamate ligase EC 6.2.1.40 4-hydroxybutyrate-CoA ligase ... tetrahydrosarcinapterin synthase EC 6.3.2.34 coenzyme F420-1:γ-L-glutamate ligase EC 6.3.2.35 D-alanine-D-serine ligase EC 6.3. ...
Cofactors, or coenzymes, are helper molecules which are needed to make an enzyme work. They are not proteins, and may be ... "Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling". Biochem. J. 323 (Pt 1): 1-12 ...
Elovson J, Vagelos PR (juli 1968). "Acyl carrier protein. X. Acyl carrier protein synthetase". J. Biol. Chem. 243 (13): 3603-11 ... Leonardi R, Zhang YM, Rock CO, Jackowski S (2005). "Coenzyme A: back in action". Progress in Lipid Research. 44 (2-3): 125-153 ... "Complete Reconstitution of the Human Coenzyme A Biosynthetic Pathway via Comparative Genomics". The Journal of Biological ... "Acyl carrier protein-specific 4'-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase". J. Biol. ...
Very long-chain acyl-coenzyme A dehydrogenase deficiency. Sanggunian[baguhin , baguhin ang source]. *. .mw-parser-output cite. ...
The acyl chains in the fatty acids are extended by a cycle of reactions that add the acyl group, reduce it to an alcohol, ... The electrons then flow through photosystem I and can then be used to reduce the coenzyme NADP+. This coenzyme can enter the ... These coenzymes are therefore continuously made, consumed and then recycled. One central coenzyme is adenosine triphosphate ( ... This reduced form of the coenzyme is then a substrate for any of the reductases in the cell that need to transfer hydrogen ...
Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA (1999). "Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA ... Very long-chain acyl-CoA synthetase is an enzyme that in humans is encoded by the SLC27A2 gene. The protein encoded by this ... Wakui K, Aoyama T, Uchiyama A, Hashimoto T, Fukushima Y (Oct 1998). "Assignment of human fatty-acid-coenzyme A ligase, very ... 2002). "Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling". J ...
Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA (Oct 1999). "Human liver-specific very-long-chain acyl-coenzyme A synthetase: ... 2000). "The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase". J. Biol. Chem. 275 (21 ... Watkins PA, Pevsner J, Steinberg SJ (2000). "Human very long-chain acyl-CoA synthetase and two human homologs: initial ...
It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid ... Other names in common use include long-chain fatty-acyl-CoA hydrolase, palmitoyl coenzyme A hydrolase, palmitoyl thioesterase, ... palmitoyl coenzyme A hydrolase, palmitoyl-CoA deacylase, palmityl thioesterase, palmityl-CoA deacylase, fatty acyl thioesterase ... A defect in acyl-CoA degradation in livers can produce hyperammonemia and hypoglycemia. Barnes EM Jr; Wakil SJ (1968). "Studies ...
Long chain FA are first activated via esterification with coenzyme A to produce a fatty acid-coA complex which can then cross ... "Structure of Human Carnitine Acetyltransferase Molecular Basis for Fatty Acyl Transfer". J. Biol. Chem. 278 (15): 13159-65. doi ...
MCPA also inhibits the dehydrogenation of a number of Acyl-CoA dehydrogenases. The inhibition of one in particular, butyryl CoA ... MCPA forms non-metabolizable esters with coenzyme A (CoA) and carnitine, causing a decrease in their bioavailability and ... it also limits Acyl and carnitine cofactors, which are instrumental in the oxidation of large fatty acids. Hypoglycin A ... dehydrogenase (a short-chain acyl-CoA dehydrogenase), causes β-oxidation to cease before fully realized, which leads to a ...
"Inhibition of glucose-6-phosphate dehydrogenase by long chain acyl-coenzyme A". Biochemical and Biophysical Research ... Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to ... The NADP+ structural site is located greater than 20Å away from the substrate binding site and the catalytic coenzyme NADP+ ... The NADP+ structural site is quite different from the NADP+ catalytic coenzyme binding site, and contains the nucleotide- ...
... and lecithin retinol acyl transferase. Higa HH, Varki A (1988). "Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1- ...
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 ...
The mupirocin pathway also contains several tandem acyl carrier protein doublets or triplets. This may be an adaptation to ... One of the AT domains from MmpC may transfer an activated acetyl group from acetyl-Coenzyme A (CoA) to the first ACP domain. ...
Matsumoto K, Fujiwara Y, Nagai R, Yoshida M, Ueda S (Feb 2008). "Expression of two isozymes of acyl-coenzyme A: cholesterol ... acetyl-Coenzyme A acetyltransferase 2) gene Acetyl-Coenzyme A acetyltransferase 2 is an acetyl-CoA C-acetyltransferase enzyme. ... "Entrez Gene: acetyl-Coenzyme A acetyltransferase 2". Human ACAT2 genome location and ACAT2 gene details page in the UCSC Genome ... cholesterol metabolism in LNCaP and PC-3 cell lines is regulated through two different isoforms of acyl-coenzyme A:Cholesterol ...
... encoding enzyme Acyl-coenzyme A synthetase ACSM2B, mitochondrial ACSM3: encoding enzyme Acyl-coenzyme A synthetase ACSM3, ... ACSF3: encoding enzyme Acyl-CoA synthetase family member 3 ACSM2B: ...
... glutamylcysteine is converted into an acyl phosphate by the transfer of an inorganic phosphate group of ATP to generate an acyl ... "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin ...
"Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ... which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. The encoded protein can also bind ... in which 3-ketoacyl CoA is cleaved by the thiol group of another molecule of Coenzyme A. The thiol is inserted between C-2 and ... "Deposition of Alzheimer's vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A ...
... an enzyme used in lipid metabolism Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD deficiency or MCADD), caused by ... MCAD may refer to: ACADM or MCAD, a gene Medium-chain acyl-CoA dehydrogenase, ...
... converts fatty acyl-CoA to fatty acyl-carnitine. Carnitine biosynthesis inhibitor: Mildronate 3-KAT inhibitors: Trimetazidine 3 ... 3-ketoacyl-coenzyme A thiolase) inhibitors directly inhibits fatty acid beta-oxidation. pFOX directly inhibits fatty acid beta- ...
By disrupting an acyl-coenzyme A (CoA) thioesterase gene, Sabirova and colleagues were able to mutate the organism to hyper- ... Hydroxyacyl-Coenzyme A-Specific Thioesterase Gene Causes Hyperproduction of Extracellular Polyhydroxyalkanoates by Alcanivorax ...
Two prominent examples are coumaroyl-coenzyme A and crotonyl-coenzyme A. They arise by the action of acyl-CoA dehydrogenases. ... Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718-25 ... it is the acyl group derived from acrylic acid. The preferred IUPAC name for the group is prop-2-enoyl, and it is also known as ...
... (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 ( ...
Formation of Cytidine-5'-trisphosphate (CTP) from UTP can be achieved by cytidylate synthetase by an acyl phosphate ... Co-enzyme N10-formyl-THF, along with enzyme GAR transformylase, then donates a one-carbon unit to the amino group onto the ...
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- ...
Bellig LL (2004). "Maternal acute fatty liver of pregnancy and the associated risk for long-chain 3-hydroxyacyl-coenzyme a ... "Disorders of mitochondrial fatty acyl-CoA beta-oxidation" (PDF). Journal of Inherited Metabolic Disease. 22 (4): 442-487. doi: ... caused by long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency. This leads to decreased metabolism of long chain fatty ...
This means that, for each round of β-oxidation, the fatty acyl-Co-A is shortened by two carbons. If the fatty acid began with ... Methylmalonyl coenzyme A racemase". The Journal of Biological Chemistry. 237 (10): 3065-8. doi:10.1016/S0021-9258(18)50121-6. ... If the fatty acid began with an odd number of carbons, however, β-oxidation would break the fatty acyl-CoA down until the three ... In the catabolism of even-chain saturated fatty acids, the β-oxidation pathway breaks down fatty acyl-CoA molecules in repeated ...
Therefore, we cloned several genes encoding fatty acyl-coenzyme A reductases from wheat and analyzed their function in yeast ... We reported the cloning and characterization of three TaFARs, namely TaFAR6, TaFAR7 and TaFAR8, encoding fatty acyl-coenzyme A ... the acyl-reduction pathway mainly participates in this process. Fatty-acyl coenzyme A reductase (FAR) is a crucial enzyme ... We reported the cloning and characterization of three TaFARs, namely TaFAR6, TaFAR7 and TaFAR8, encoding fatty acyl-coenzyme A ...
Peroxisomal acyl-coenzyme A oxidase 2 protein, Protein Peroxisomal acyl-coenzyme A oxidase 2, Mouse Peroxisomal acyl-coenzyme A ... Mouse Peroxisomal acyl-coenzyme A oxidase 2, Mouse protein Peroxisomal acyl-coenzyme A oxidase 2 ... Peroxisomal acyl-coenzyme A oxidase 2, THCCox protein, Protein THCCox, Mouse THCCox Protein, Mouse THCCox, Mouse protein THCCox ... Mouse Acyl Coenzyme A Oxidase 2, Branched (ACOX2) Protein. Mouse Acyl Coenzyme A Oxidase 2, Branched (ACOX2) Protein. ...
The purified protein did not require divalent metals, molecular oxygen or any cosubstrates or coenzymes for activity. The ... reaction is part of a widely distributed new principle of aerobic aromatic metabolism in which all intermediates are coenzyme A ... Acyl Coenzyme A * Bacterial Proteins * Esters * Semicarbazides * Sulfhydryl Compounds * benzoyl-coenzyme A ...
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 ...
Role of acyl-coenzyme A: cholesterol transferase 1 (ACAT1) in retinal neovascularization.. Zaidi, Syed A H; Lemtalsi, Tahira; ... during ischemic retinopathy by targeting the cholesterol metabolizing enzyme acyl-coenzyme A cholesterol transferase 1 (ACAT1 ...
Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme) 17295914, ... MSMEG_6179 MSMEG_6179 Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating ...
CES1 (Liver Carboxylesterase 1, Acyl-coenzyme A:cholesterol Acyltransferase, ACAT, Brain Carboxylesterase hBr1, Cocaine ... CES1 (Liver Carboxylesterase 1, Acyl-coenzyme A:cholesterol Acyltransferase, ACAT, Brain Carboxylesterase hBr1, Cocaine ...
Acyl-coenzyme A (acyl-CoA) synthetases - Fatty acid synthesis. In addition, a cascade of enzymes is involved in beta-oxidation ...
... long-chain acyl-CoA synthetase gene; MCP1, monocyte chemoattractant protein 1; F4/80, a marker of monocytes; p38, mitogen- ... hydroxymethylglutaryl coenzyme A reductase; Ldlr, low-density lipoprotein receptor gene; Pnpla2, adipose triglyceride lipase ...
Medium-chain acyl-coenzyme A dehydrogenase deficiency: clinical course in 120 affected children. J Pediatr 1994;124:40915. ... MCAD and MCADD are used interchangeably to refer to medium-chain acyl-CoA dehydrogenase deficiency. A task force of ... Medium chain acyl Co-A dehydrogenase deficiency human genome epidemiology review. Genetics in Medicine 1999;1:3329. ... Diagnostic and therapeutic implications of medium-chain acylcarnitines in the medium-chain acyl-CoA dehydrogenase deficiency. ...
acyl-coenzyme A thioesterase 1/2/4 [EC:3.1.2.2]. K01071 medium-chain acyl-[acyl-carrier-protein] hydrolase [EC:3.1.2.21]. ... acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase / long-chain-fatty-acid--[acyl-carrier-protein] ligase [EC:2.3.1.40 ... medium-chain acyl-CoA ligase / lipoate-activating enzyme [EC:6.2.1.2]. K24012 acetate---CoA ligase (ADP-forming) [EC:6.2.1.13] ... medium-chain-fatty-acid---[acyl-carrier-protein] ligase [EC:6.2.1.47]. K21182 (S)-beta-tyrosine adenylation enzyme [EC:6.2.1.-] ...
Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. Watkins PA, et al. J Lipid Res, 2007 Dec. PMID ... acyl-CoA synthetase family member 4. non-ribosomal peptide synthetase 1098. non-ribosomal peptide synthetase 998. NP_ ... Title: Vertebrate Acyl CoA synthetase family member 4 (ACSF4-U26) is a β-alanine-activating enzyme homologous to bacterial non- ... Vertebrate Acyl CoA synthetase family member 4 (ACSF4-U26) is a β-alanine-activating enzyme homologous to bacterial non- ...
Acyl-coenzyme A binding protein expression is fibre-type specific in rat skeletal muscle but not affected by moderate endurance ... Acyl-CoA binding protein expression is fiber type-specific and elevated in muscles from the obese insulin-resistant Zucker rat ...
PR:000004544 acyl-coenzyme A thioesterase 10, mitochondrial. (term hierarchy). * EC. 3.1.2.- ...
Management Principles for Acute Illness in Patients With Medium-Chain Acyl-Coenzyme A Dehydrogenase Deficiency. MCADD RELATED: ... Abstract Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCADD) is a fatty acid oxidation disorder in which the patient ... Coenzyme Q10 could treat mitochondrial diseases, colon cancer, thyroid carcinoma and Crohns disease. Graphic overview of the ... Credit: University of Granada Coenzyme Q10 (CoQ10) is a molecule essential for life that is synthesized in the cells of our ...
Name: acyl-Coenzyme A binding domain containing 6. Synonyms: 0610010G04Rik, 2610100E10Rik. Type: Gene ...
Medium chain acyl-coenzyme A dehydrogenase deficiency. *Prevalence: 1-9 / 100 000 ... Medium chain acyl-CoA dehydrogenase deficiency. Disease definition Medium chain acyl-CoA dehydrogenase (MCAD) deficiency (MCADD ... Differential diagnosis includes other disorders of mitochondrial fatty acid oxidation including multiple acyl-CoA dehydrogenase ...
Crystal Structure of the Complex Between Mycobacterium Tuberculosis Beta-Ketoacyl-Acyl Carrier Protein Synthase III and Lauroyl ... with lauroyl-coenzyme A. J.Mol.Biol. (2005) Release Date. 2005-03-22. Peptides. 3-oxoacyl-[acyl-carrier-protein] synthase III: ... of the Complex Between Mycobacterium Tuberculosis Beta-Ketoacyl-Acyl Carrier Protein Synthase III and Lauroyl Coenzyme A ... Musayev, F. et al., Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein ...
"Fibrates downregulate apolipoprotein C-III expression independent of induction of peroxisomal acyl coenzyme A oxidase. A ... It converts acyl-carnitine to acyl-CoA and is strongly upregulated by PPAR. agonists [33]. Most of the genes of FA metabolism ... activation, such as acyl-CoA synthetase (Acs) coding for an enzyme responsible for activation of FA to their fatty acyl-CoA ... target gene, acyl-CoA oxidase 1 (Acox1) encodes the rate-limiting enzyme of this process [40]. After ACOX1 has introduced a ...
Preservation of Acyl Coenzyme A Attenuates Pathological and Metabolic Cardiac Remodeling through Selective Lipid Trafficking. ... Acylcarnitines are thought to increase as a result of reduced or impaired catabolism of acyl-CoAs. Additionally, if pathways ... As acylcarnitine concentrations mirror the amount of acyl-CoA within the mitochondria, this most likely reflects a reduction in ... If β-oxidation is impaired, fatty acyl-coAs accumulate in cytosolic and mitochondrial pools, subsequently increasing the ...
... acyl-coenzyme A (CoA), and 20% free fatty acids. All three chemical forms of beta-hydroxypalmitate were found in both the ... of the incremental long-chain acyl-CoA, whereas beta-hydroxypalmitoylcarnitine and b-hydroxystearoylcarnitine constituted 8% of ...
Teilum, K., Kragelund, B., and Poulsen, F. (2002). Transient structure formation in unfolded acyl-coenzyme A-binding protein ...
Corbicula fluminea; active ingredients; acyl coenzyme A; alanine transaminase; aspartate transaminase; beta oxidation; ...
... coa-coenzyme A; dag-diacylglycerol; g3p-glyceraldehyde 3-phosphate; oaa-oxaloacetate; IsoCit-Isocitrate; malacp-malonyl acyl ... acp-acyl carrier protein; c8:0acp-octanoyl acyl carrier protein; c10:0acp-decanoyl acyl carrier protein; c12:0acp-dodecanoyl ... acyl carrier protein; c14:0acp-tetradecanoyl acyl carrier protein; c16:0acp-Hexadecanoyl acyl carrier protein; c16:0coa- ... 1agpg-1-Acyl-sn-glycero-3-phosphoglycerol; 2OG-2-oxoglutarate; acald-acetaldehyde; accoa-acetyl-CoA; aconC-cis-aconitate; ...
Peroxisomal acyl-coenzyme A oxidase 1. Molecular Weight. 74423.035 Da. References. *Dyall SC: Long-chain omega-3 fatty acids ... Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl ...
Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11). 3h3q. Crystal structure of the CERT START domain in complex ...
... and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates ... Interaction of acyl coenzyme A substrates and analogues with pig kidney medium-chain acyl-coA dehydrogenase ... Contribution of the distal pocket residue to the acyl-chain-length specificity of (R)-specific enoyl-coenzyme A hydratases from ... The purification and some properties of electron transfer flavoprotein and general fatty acyl coenzyme A dehydrogenase from pig ...
  • Medium chain acyl-CoA dehydrogenase (MCAD) deficiency (MCADD) is an inborn error of mitochondrial fatty acid oxidation characterized by a rapidly progressive metabolic crisis, often presenting as hypoketotic hypoglycemia, lethargy, vomiting, seizures and coma, which can be fatal in the absence of emergency medical intervention. (orpha.net)
  • Differential diagnosis includes other disorders of mitochondrial fatty acid oxidation including multiple acyl-CoA dehydrogenase deficiency (MADD) (see this term). (orpha.net)
  • ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. (prospecbio.com)
  • Four genes were identified in mouse, namely cytosolic acyl-CoA thioesterase (mCTE-I), mitochondrial acyl-CoA thioesterase (mMTE-I), and two peroxisomal acyl-CoA thioesterases (mPTE-la and -Ib), located in a cluster on mouse chromosome 12. (avhandlingar.se)
  • Mitochondrial acyl-CoA dehydrogenase family member 9 (ACAD9) is essential for the assembly of mitochondrial respiratory chain complex I. Disease causing biallelic variants in ACAD9 have been reported in individuals presenting with lactic acidosis and cardiomyopathy. (biomedcentral.com)
  • Impact of short- and medium-chain organic acids, acylcarnitines, and acyl-CoAs on mitochondrial energy metabolism. (medscape.com)
  • 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)
  • These acyl-CoA thioesterases showed sequence similarity only to the bile acid-CoA:amino acid N- acyltransferase involved in conjugation of bile acids to glycine or taurine. (avhandlingar.se)
  • Lecithin:Cholesterol acyltransferase (LCAT) is found in peripheral tissues and utilizes phosphatidylcholine as the source of acyl chains. (sigmaaldrich.com)
  • In the lumen, dietary cholesterol absorbed by enterocytes is esterified by acyl-coenzyme A: cholesterol acyltransferase 2 (ACAT2), which is found in both the intestine and liver ( Figure 2 ). (sigmaaldrich.com)
  • Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT2) is found in the liver and intestine, and utilizes acyl-CoA as the source of acyl chains. (sigmaaldrich.com)
  • MS/MS technology expands the metabolic disorder screening panel (i.e., the number of disorders that can be detected) by incorporating an acylcarnitine profile, which enables detection of fatty acid oxidation disorders (e.g., medium-chain acyl-CoA dehydrogenase [MCAD] deficiency) ( 7-10 ) and other organic acid disorders. (cdc.gov)
  • MCADD RELATED: Abstract Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCADD) is a fatty acid oxidation disorder in which the patient is unable to break down fats to produce energy. (mitoaction.org)
  • Mutations in ACADS have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency. (prospecbio.com)
  • Multiple acyl-CoA dehydrogenase deficiency (MADD), also known as glutaric acidemia Type II, is a rare autosomal recessive defect of the electron transfer flavoprotein or ubiquinone oxidoreductase, resulting in abnormal fatty acid, amino acid, and choline metabolism. (helmholtz-muenchen.de)
  • Measurement of serum electrolyte levels may reveal depressed bicarbonate and an anion gap in medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) deficiency. (medscape.com)
  • 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)
  • Risk stratification by residual enzyme activity after newborn screening for medium-chain acyl-CoA dehyrogenase deficiency: data from a cohort study. (medscape.com)
  • Abnormal screening in a healthy infant of a mother with undiagnosed medium-chain acyl-coA dehydrogenase deficiency. (medscape.com)
  • beta-Ketoacyl-ACP synthases (KAS) are the condensing enzymes present in the fatty acid biosynthesis pathway and are able to elongate an acyl chain bound to either co-enzyme A (CoA) or acyl carrier protein (ACP) with a two-carbon unit derived from malonyl-ACP. (rcsb.org)
  • Synthesis of pantothenate (Vitamine B5), which is a precursor of the acyl carrier coenzyme A, is an example of such a pathway. (umn.edu)
  • ACL is an enzyme upstream of 3-hydroxy-3-methyl-glutaryl-coenzyme A (HMG-CoA) reductase in the cholesterol biosynthesis pathway. (medscape.com)
  • LCAT and ACAT also differ in the sources they use for the acyl chains. (sigmaaldrich.com)
  • LCAT uses phosphatidylcholine while ACAT uses acyl-CoA. (sigmaaldrich.com)
  • Then, using C 16 and C 18 acyl-CoA and malonyl-CoA as substrates, the fatty acid elongase (FAE) complex performs a reiterative cycle of four reactions catalyzed by a β-ketoacyl-CoA synthase (KCS), a β-ketoacyl-CoA reductase (KCR), a β-hydroxyacyl-CoA dehydratase (HCD), and an enoyl-CoA reductase (ECR) to synthesize saturated very-long-chain fatty acids (VLCFAs) [ 17 ]. (biomedcentral.com)
  • Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. J.Mol.Biol. (expasy.org)
  • 1E5M: Beta ketoacyl acyl carrier protein synthase II (KASII) from Synechocystis sp. (rcsb.org)
  • Beta ketoacyl acyl carrier protein synthase II (KASII) from Synechocystis sp. (rcsb.org)
  • Ceramide synthase component, involved in synthesis of ceramide from C26(acyl)-coenzyme A and dihydro. (yeastrc.org)
  • We have also identified a further acyl-CoA thioesterase, peroxisomal acyl-CoA thioesterase 2, PTE-2, as a novel PPARalpha target gene, and have shown that this enzyme acts as a 'general' acyl-CoA thioesterase in peroxisomal lipid metabolism. (avhandlingar.se)
  • Functional characterization of thioesterase superfamily member 1/Acyl-CoA thioesterase 11: implications for metabolic regulation. (harvard.edu)
  • Vertebrate Acyl CoA synthetase family member 4 (ACSF4-U26) is a β-alanine-activating enzyme homologous to bacterial non-ribosomal peptide synthetase. (nih.gov)
  • Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana. (mpg.de)
  • Therefore, we cloned several genes encoding fatty acyl-coenzyme A reductases from wheat and analyzed their function in yeast and plants. (biomedcentral.com)
  • Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. (nih.gov)
  • We have now cloned and characterized a family of acyl-CoA thioesterase genes in mouse and human, which show a high degree of sequence similarity. (avhandlingar.se)
  • Acyl-Carrier Protein S-Malonyltransferase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
  • 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. (ucdenver.edu)
  • This graph shows the total number of publications written about "Acyl-Carrier Protein S-Malonyltransferase" by people in this website by year, and whether "Acyl-Carrier Protein S-Malonyltransferase" was a major or minor topic of these publications. (ucdenver.edu)
  • Below are the most recent publications written about "Acyl-Carrier Protein S-Malonyltransferase" by people in Profiles. (ucdenver.edu)
  • Here we show that production of retinyl esters by lecithin:retinol acyl transferase (LRAT) in yeast cells, incapable of producing triacylglycerols and steryl esters, causes the formation of lipid droplets. (biorxiv.org)
  • 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. (harvard.edu)
  • The purified protein did not require divalent metals, molecular oxygen or any cosubstrates or coenzymes for activity. (nih.gov)
  • 1, 2] Lipid substrates share a common structure, including a ceramide backbone (2-N-acyl-sphingosine), in which various sphingolipids are derived by substitution of hexoses, phosphorylcholine, or one or more sialic acid residues on terminal hydroxyl groups of the ceramide molecule. (medscape.com)
  • 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. (bvsalud.org)
  • Recently, this was weakened by a double-blind randomized crossover study of bezafibrate in five individuals with acyl-CoA dehydrogenase very long chain (ACADVL) deficiencies in whom no improvement could be detected [ 11 ]. (biomedcentral.com)
  • Pantothenic acid is a precursor of coenzyme A (CoA), an important cofactor and acyl group carrier in cells. (depkewellness.com)
  • Resistant parasites generated in vitro showed mutations in acetyl-coenzyme A synthetase and acyl-coenzyme A synthetase 11. (elsevier.com)
  • The complex reaction is part of a widely distributed new principle of aerobic aromatic metabolism in which all intermediates are coenzyme A thioesters and the actual ring-cleavage reaction does not require molecular oxygen. (nih.gov)
  • Metabolomics revealed that coenzyme A biosynthetic enzymes converted pantothenamides into coenzyme A analogs that interfered with parasite acetyl-coenzyme A anabolism. (elsevier.com)
  • Role of acyl-coenzyme A: cholesterol transferase 1 (ACAT1) in retinal neovascularization. (bvsalud.org)
  • We have investigated the efficacy of a new strategy to limit pathological retinal neovascularization (RNV) during ischemic retinopathy by targeting the cholesterol metabolizing enzyme acyl- coenzyme A cholesterol transferase 1 (ACAT1). (bvsalud.org)
  • Our work involves characterization of a group of acyl-CoA thioesterase enzymes, that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH). (avhandlingar.se)
  • Three endoplasmic reticulum-associated fatty acyl-coenzyme a reductases were involved in the production of primary alcohols in hexaploid wheat (Triticum aestivum L. (biomedcentral.com)
  • After 10 min of ischemia beta-hydroxypalmitoyl-CoA and beta-hydroxystearoyl-CoA constituted at least 16% of the incremental long-chain acyl-CoA, whereas beta-hydroxypalmitoylcarnitine and b-hydroxystearoylcarnitine constituted 8% of the incremental long-chain acylcarnitine. (jci.org)
  • ACAD9 is most homologous (47% amino acid identity, 65% amino acid similarity) to very long-chain acyl-CoA dehydrogenase (VLCAD). (biomedcentral.com)
  • Bempedoic acid and its active metabolite, ESP15228, require coenzyme A (CoA) activation by very long?chain acyl-CoA synthetase 1 (ACSVL1) to ETC-1002-CoA and ESP15228-CoA, respectively. (medscape.com)
  • Both acids were activated with coenzyme A in a Mg 2+ - and ATP-dependent reaction. (microbiologyresearch.org)
  • IMSEAR at SEARO: Differential binding of NAD+ to acyl glyceraldehyde-3-phosphate dehydrogenase and its role in the acyl group transfer reaction. (who.int)
  • Initial rates of the NAD(+)-dependent reaction of di-FA-GPDH with arsenate and phosphate and of mono-FA-GPDH with phosphate have been determined at varying coenzyme concentrations. (who.int)
  • The data suggest that binding of NAD+ at the tight sites does not activate the acyl group for its reaction with the acceptor (phosphate or arsenate). (who.int)
  • The group transfer reaction is dependent only on NAD+ binding to the loose sites, which carry the acyl group. (who.int)
  • Lipid fractionation studies showed that by 10 min these two beta-hydroxy fatty acids were distributed approximately as 60% acylcarnitine, 20% acyl-coenzyme A (CoA), and 20% free fatty acids. (jci.org)
  • ACADs belong to a family of flavoenzymes involved in the ß-oxidation of acyl-CoA and amino acid catabolism. (biomedcentral.com)
  • The acyl-CoA thioesterase I is regulated by PPARalpha and HNF4alpha via a distal response element in the promoter. (harvard.edu)
  • Acyl-CoA dehydrogenase, Domain of unknown function (DUF1974) [Interproscan]. (ntu.edu.sg)
  • The variation in the acyl-carrier (ACP or CoA) specificity might also be connected to this classification and residues involved in ACP binding in structure class 2 can be suggested based on the comparison. (rcsb.org)
  • C6-C10-dicarboxylic aciduria: investigations of a patient with riboflavin responsive multiple acyl-CoA dehydrogenation defects. (medscape.com)