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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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.
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. ...
3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ ⇌. {\displaystyle \rightleftharpoons }. 3-oxoacyl-[acyl-carrier-protein] + ... Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP ... In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. ...
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. ...
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 ...
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. Biology portal 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 ...
ACSM2B: encoding enzyme Acyl-coenzyme A synthetase ACSM2B, mitochondrial. *ACSM3: encoding enzyme Acyl-coenzyme A synthetase ... ACSF3: encoding enzyme Acyl-CoA synthetase family member 3. * ...
... (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ... 1993). "Medium-Chain Acyl-Coenzyme A Dehydrogenase Deficiency". PMID 20301597.. *^ Gregersen N, Andresen BS, Bross P, Winter V ... Medium-chain acyl-coenzyme A dehydrogenase deficiency can be caused by mutations in the ACADM gene. More than 30 ACADM gene ... The acyl-coenzyme A dehydrogenase for medium-chain fatty acids (ACADM) enzyme is essential for converting these particular ...
Very long-chain acyl-coenzyme A dehydrogenase deficiency. Cytogenetic band[edit]. .mw-parser-output .tmulti .thumbinner{display ...
ACADVL: acyl-coenzyme A dehydrogenase, very long chain (17p13.1). *SHBG: Sex hormone binding globulin (17p13.1) ...
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 ...
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): ...
Overview of all the structural information available in the PDB for UniProt: Q86TX2 (Acyl-coenzyme A thioesterase 1) at the ... 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 ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, acyl-CoA thioester hydrolases, and palmitoyl ...
"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 ... Diglyceride acyltransferase (or O-acyltransferase), DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl ... "Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis". ...
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 ...
... 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. ...
... 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 ...
... 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 ...
Enoyl-acyl carrier protein reductase/Enoyl ACP reductase. *7-Dehydrocholesterol reductase. *Biliverdin reductase ...
2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ... "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ... transferase activity, transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase activity. • long-chain-3- ... transferase activity, transferring acyl groups. • 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C- ...
Wagner AL (1975). 》Vitamins and Coenzymes》. Krieger Pub Co. ISBN 0-88275-258-8. .. ... "Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling". 》The Biochemical Journal》 ...
coenzyme yield ATP yield Source of ATP Glycolysis preparatory phase −2 Phosphorylation of glucose and fructose 6-phosphate uses ... The citric acid cycle is an 8-step process involving 18 different enzymes and co-enzymes.[6] During the cycle, acetyl-CoA (2 ... It is assumed that all the reduced coenzymes are oxidized by the electron transport chain and used for oxidative ... From the complete oxidation of one glucose molecule to carbon dioxide and oxidation of all the reduced coenzymes. ...
Fatty acyl CoA dehydrogenase requires FAD in fatty acid oxidation. *FAD is required to convert retinol (vitamin A) to retinoic ... Riboflavin functions as a coenzyme, meaning that it is required for enzymes (proteins) to perform normal physiological actions ... The primary coenzyme form of vitamin B6 (pyridoxal phosphate) is FMN dependent ...
Amino+Acyl-tRNA+Synthetases at the US National Library of Medicine Medical Subject Headings (MeSH) ... Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ...
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 ...
The electron is eventually used to reduce the co-enzyme NADP with a H+ to NADPH (which has functions in the light-independent ...
Glycerol-3-phosphate is first acylated with acyl-coenzyme A (acyl-CoA) to form lysophosphatidic acid, which is then acylated ... with another molecule of acyl-CoA to yield phosphatidic acid. Phosphatidic acid is then de-phosphorylated to form ...
... β2 Heterotetrameric Acyl Coenzyme A Dehydrogenase Family". J. Bacteriol. 195 (19): 4331-4341. doi:10.1128/JB.00502-13. PMC ...
2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ... Crystal structure of Tetrahymena Gcn5 with bound coenzyme A and histone H3 peptide (PDB 1QSN). The central core (green), ... flanking N- and C-terminal segments (blue), coenzyme A (orange), and histone peptide (red) are shown. ...
Biochemical functions of coenzyme Q10. „Journal of the American College of Nutrition". 20 (6), s. 591-8, 2001. PMID: 11771674. ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase. „J. Biol. Chem.". 258 (2), s. 1066-76, 1983. PMID: ... Lenaz G. A critical appraisal of the mitochondrial coenzyme Q pool. „FEBS Lett.". 509 (2), s. 151-5, 2001. DOI: 10.1016/S0014- ... Ikeda Y, Dabrowski C, Tanaka K. Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria ...
PLP aids in the synthesis of hemoglobin, by serving as a coenzyme for the enzyme ALA synthase.[6] It also binds to two sites on ... which is combined with a fatty acyl-CoA to form dihydroceramide. Dihydroceramide is then further desaturated to form ceramide. ... Its active form, pyridoxal 5′-phosphate, serves as a coenzyme in some 100 enzyme reactions in amino acid, glucose, and lipid ... PLP is a coenzyme needed for the proper function of the enzymes cystathionine synthase and cystathionase. These enzymes ...
The carnitine also assists in the removal of acyl-CoA, buildup of which is common in low-protein diets by converting it into ... The inherited forms of methylmalonic acidemia cause defects in the metabolic pathway where methylmalonyl-coenzyme A (CoA) is ... acyl-carnitine which can be excreted in urine. Though not all forms of methylmalonyl acidemia are responsive to cobalamin, ...
Molecular Characterization of a Major Plastidial Acyl-Coenzyme a Synthetase from Arabidopsis". Plant Physiology. 129 (4): 1700- ...
Transfer of acyl groups or acyl groups that become alkyl groups during the process of being transferred are key aspects of EC ... ChAT functions to transfer an acetyl group from acetyl co-enzyme A to choline in the synapses of nerve cells and exists in two ... Further, this category also differentiates between amino-acyl and non-amino-acyl groups. Peptidyl transferase is a ribozyme ... The donor is often a coenzyme. Some of the most important discoveries relating to transferases occurred as early as the 1930s. ...
Fatty acids are first converted to acyl-CoA. Acyl-CoA is then degraded in a four-step cycle of dehydrogenation, hydration, ... Coenzyme A (CoASH or CoA) consists of a β-mercaptoethylamine group linked to the vitamin pantothenic acid through an amide ... Acetyl-CoA (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid ... Acetyl+Coenzyme+A at the US National Library of Medicine Medical Subject Headings (MeSH) ...
2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A acetyltransferase ... transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer. • citrate (Si)-synthase activity ... Citrate synthase catalyzes the condensation reaction of the two-carbon acetate residue from acetyl coenzyme A and a molecule of ... Two binding sites can be found therein: one reserved for citrate or oxaloacetate and the other for Coenzyme A. The active site ...
... is produced which is a building block for new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to ... The color scheme is as follows: enzyme, coenzymes, substrate names, metal ions, phosphate, and carbonate ... Other allosteric activators include glutamate and other dicarboxylic acids.[16] Long and short chain fatty acyl CoAs are ... Tong L (August 2005). "Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery". ...
Acyl carrier protein. *Adaptor protein. *Cholesterylester transfer protein. *F-box protein. *GTP-binding protein ...
中鏈乙醯輔酶A脫氫酶缺乏症(英语:medium-chain acyl-coenzyme A dehydrogenase deficiency)(MCADD)[42] ...
NADH-coenzyme Q oxidoreductase (complex I)Edit. Complex I or NADH-Q oxidoreductase. The abbreviations are discussed in the text ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066-76. PMID 6401712. ... produce the reduced coenzyme NADH. This coenzyme contains electrons that have a high transfer potential; in other words, they ... NADH-coenzyme Q oxidoreductase, also known as NADH dehydrogenase or complex I, is the first protein in the electron transport ...
This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:5-phosphoribosyl-5-amino-4-imidazole-carb oxamide N-formyltransferase. Other names in common use include: ...
Crane FL (2001년 12월 1일). "Biochemical functions of coenzyme Q10". 《J Am Coll Nutr》 20 (6): 591-8. doi:10.1080/07315724.2001. ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". 《J. Biol. Chem.》 258 (2): 1066-76. PMID 6401712. 29 ... Lenaz G (2001). "A critical appraisal of the mitochondrial coenzyme Q pool". 《FEBS Lett.》 509 (2): 151-5. doi:10.1016/S0014- ... "Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. ...
Glutamine is formed if an ammonium ion attacks the acyl-phosphate intermediate, while glutamate is remade if water attacks the ... Isovaleryl coenzyme A dehydrogenase. *α-Ketoisocaproate dioxygenase. *Leucine 2,3-aminomutase. *Methylcrotonyl-CoA carboxylase ... Ammonium binds strongly to GS only if the acyl-phosphate intermediate is present. Ammonium, rather than ammonia, binds to GS ... ATP phosphorylates glutamate to form ADP and an acyl-phosphate intermediate, γ-glutamyl phosphate, which reacts with ammonia, ...
m6A and m4C methyltransferases are found primarily in prokaryotes (although recent evidence has suggested that m6A is abundant in eukaryotes[1]). m5C methyltransfereases are found in some lower eukaryotes, in most higher plants, and in animals beginning with the echinoderms. The m6A methyltransferases (N-6 adenine-specific DNA methylase) (A-Mtase) are enzymes that specifically methylate the amino group at the C-6 position of adenines in DNA. They are found in the three existing types of bacterial restriction-modification systems (in type I system the A-Mtase is the product of the hsdM gene, and in type III it is the product of the mod gene). These enzymes are responsible for the methylation of specific DNA sequences in order to prevent the host from digesting its own genome via its restriction enzymes. These methylases have the same sequence specificity as their corresponding restriction enzymes. These enzymes contain a conserved motif Asp/Asn-Pro-Pro-Tyr/Phe in their N-terminal section, this ...
Dozens of ATP equivalents are generated by the beta-oxidation of a single long acyl chain.[20] The acetyl-CoA produced by beta- ... It is used in cells as a coenzyme.. Contents. StructureEdit. In terms of its structure, ATP consists of an adenine attached by ...
Here they can be oxidized and combined with coenzyme A to form CO2, acetyl-CoA, and NADH, as in the normal cycle.[36] ... Acyl-CoA is oxidized to trans-Enoyl-CoA while FAD is reduced to FADH2, which is similar to the oxidation of succinate to ... Structural diagram of acetyl-CoA: The portion in blue, on the left, is the acetyl group; the portion in black is coenzyme A. ... FADH2, therefore, facilitates transfer of electrons to coenzyme Q, which is the final electron acceptor of the reaction ...
PREDICTED: acyl-coenzyme A thioesterase 9, mitochondrial isoform X1 [Aquila chry... PREDICTED: acyl-coenzyme A thioesterase 9, ... PREDICTED: acyl-coenzyme A thioesterase 9, mitochondrial isoform X1 [Aquila chrysaetos canadensis]. NCBI Reference Sequence: XP ...
Short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD), is an autosomal recessive fatty acid oxidation disorder which ... The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic ... Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy ( ... Short-Chain Acyl-Coenzyme A Dehydrogenase Deficiency". Molecular Genetics and Metabolism (Free full text). 95 (4): 195-200. doi ...
Hegyi, T.; Ostfeld, B.; Gardner, K. (1992). "Medium chain acyl-coenzyme a dehydrogenase deficiency and SIDS". New Jersey ... Wilcken, B.; Hammond, J.; Silink, M. (1994-05-01). "Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase ... "Medium-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". PMID 20301597. Cite journal requires ,journal= (help) Leydiker, K. B.; ... Medium-chain acyl-CoA dehydrogenase deficiency (MCAD deficiency or MCADD), is a disorder of fatty acid oxidation that impairs ...
Matern, D.; Rinaldo, P.; Pagon, R. A.; Bird, T. D.; Dolan, C. R.; Stephens, K.; Adam, M. P. (1993). "Medium-Chain Acyl-Coenzyme ... Hegyi, T.; Ostfeld, B.; Gardner, K. (1992). "Medium chain acyl-coenzyme a dehydrogenase deficiency and SIDS". New Jersey ... Redirected from Medium-chain acyl-CoA dehydrogenase deficiency). Medium-chain acyl-CoA dehydrogenase deficiency, often known as ... "Morbidity and mortality in medium chain acyl coenzyme A dehydrogenase deficiency". Archives of Disease in Childhood. 70 (5): ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
midway encodes an acyl coenzyme A: diacylglycerol acyl-transferase: The two midway alleles, mdyqx25 and mdyrf48, were mapped to ... Characterization of the midway locus reveals that the gene encodes a protein with a high degree of similarity to acyl coenzyme ... 1997 Acyl-coenzyme A. Cholesterol acyltransferase. Annu. Rev. Biochem. 66: 613-638. ... Mutations in the midway Gene Disrupt a Drosophila Acyl Coenzyme A: Diacylglycerol Acyltransferase. Michael Buszczak, Xiaohui Lu ...
... (MCAD) ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD deficiency) *Short-chain acyl-coenzyme A dehydrogenase deficiency ( ... Very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCAD deficiency) *Long-chain 3-hydroxyacyl-coenzyme A dehydrogenase ... Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCAD). Classification & external resources ICD-9 277.85 ...
Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3- ... providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. ... Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ... Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ...
Compare Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA Kits from leading suppliers on Biocompare. View specifications, prices, ... Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody- ... Your search returned 24 Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA ELISA Kit across 1 supplier. ...
Medium-chain acyl-CoA dehydrogenase deficiency, often known as MCAD deficiency or MCADD, is a disorder of fatty acid oxidation ... Retrieved from "https://www.SNPedia.com/index.php?title=Medium-chain_acyl-coenzyme_A_dehydrogenase_deficiency&oldid=1202172" ...
It is unclear if human acyl-coenzyme A thioesterase 6/ACOT6 has an acyl-CoA thioesterase (Probable). ... providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH (PubMed:16940157). ... Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ... Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ...
Acetyl coenzyme A acetyltransferase · Acyl coenzyme A desaturase 1 · Acyl coenzyme A oxidase · Apolipoprotein A4 · ... acyl coenzyme A desaturase · acyl coenzyme A desaturase 1 · adenovirus vector · fatty acid synthase · glycerol 3 phosphate ... Chemicals / CAS: acyl coenzyme A desaturase, 9014-34-0; fatty acid synthase, 9045-77-6; glycerol 3 phosphate acyltransferase, ...
View mouse Acbd3 Chr1:180726043-180754204 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
1986) A Model for Studying Membrane Fatty Acid Transport : Acyl-Coenzyme a Synthesis in Human Erythrocyte Ghosts. In: Freysz L ... A Model for Studying Membrane Fatty Acid Transport : Acyl-Coenzyme a Synthesis in Human Erythrocyte Ghosts. ... Most cells undergo de novo synthesis of acyl chains. However, all tissues take up preformed long chain saturated, ...
Acyl-Coenzyme A-Cholesterol Acyltransferase Activity in Human Liver S. Balasubramaniam ; S. Balasubramaniam ... S. Balasubramaniam, K. A. Mitropoulos, N. B. Myant, M. Mancini, A. Postiglione; Acyl-Coenzyme A-Cholesterol Acyltransferase ... thus demonstrating the presence of acyl-coenzyme A-cholesterol acyltransferase (cholesterol acyltransferase) in human liver. ...
Subtle structural response to ligand binding revealed by residual dipolar coupling refined NMR structures of acyl coenzyme A ... Acyl-CoA binding protein-like Acyl-CoA binding protein Acyl-CoA binding protein Acyl-CoA binding protein Cow (Bos taurus) [ ... RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP. ...
Multiple Acyl Coenzyme A Dehydrogenase Deficiency*Multiple Acyl Coenzyme A Dehydrogenase Deficiency ... "Multiple Acyl Coenzyme A Dehydrogenase Deficiency" by people in Harvard Catalyst Profiles by year, and whether "Multiple Acyl ... "Multiple Acyl Coenzyme A Dehydrogenase Deficiency" is a descriptor in the National Library of Medicines controlled vocabulary ... Below are the most recent publications written about "Multiple Acyl Coenzyme A Dehydrogenase Deficiency" by people in Profiles. ...
Chicken Malonyl coenzyme A acyl carrier protein transacylase mitochondrial MCAT ELISA Kit - Gentaur.com - Product info ... Chicken Malonyl coenzyme A acyl carrier protein transacylase mitochondrial MCAT ELISA Kit. Chicken Malonyl coenzyme A acyl ... Malonyl coenzyme A acyl carrier protein transacylase ELISA kit for detection of Chicken Malonyl coenzyme A acyl carrier protein ... Chicken Malonyl coenzyme A acyl carrier protein transacylase, mitochondrial (MCAT) ELISA Kit Suppplier: abebio. Price: 816.11 ...
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 … ... enzyme that uses cholesterol and long chain fatty acyl-CoA as ... Acyl-coenzyme A: cholesterol acyltransferase inhibitor Avasimibe affect survival and proliferation of glioma tumor cell lines ... Acyl-CoA: cholesterol acyltransferase (ACAT) is an intracellular membrane-bound ...
Inhibition of acyl coenzyme A:cholesterol acyltransferase (ACAT) activity in rat liver microsome. ...
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ... Cervonyl coenzyme A + Water → Coenzyme A + Docosahexaenoic acid. details Gamma-linolenoyl-CoA + Water → Coenzyme A + gamma- ... Showing Protein Cytosolic acyl coenzyme A thioester hydrolase (HMDBP01046). IdentificationBiological propertiesGene properties ... Linoleoyl-CoA + Water → Coenzyme A + Linoleic acid. details Alpha-Linolenoyl-CoA + Water → Coenzyme A + alpha-Linolenic acid. ...
Rat Acyl coenzyme A ELISA Kit is available 14 times from supplier ab-elisa elisas at Gentaur.com shop ... Rat Acyl coenzyme A ELISA Kit product information; ... Rat Acyl coenzyme A ELISA Kit. Rat Acyl coenzyme A ELISA Kit is ... Short name Acyl-coenzyme A thioesterase 12 (ACOT12) ELISA Kit Alternative name ELISA kit for Rat Acyl-coenzyme A thioesterase ... AE23453RA , Rat Acyl-coenzyme A thioesterase 12 (ACOT12) ELISA Kit size: 96 wells plate , 916.80 USD Catalog number AE23453RA ...
To enter the β-oxidation pathway, fatty acids need to be activated to acyl-coenzyme As (CoAs) by the enzyme acyl-CoA synthetase ... and characterization of a novel pumpkin short-chain acyl-coenzyme A oxidase with structural similarity to acyl-coenzyme A ... Molecular characterization of a major plastidial acyl-coenzyme A synthetase from Arabidopsis. Plant Physiol 129:1700-1709. ... 1997) Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that ...
Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: a possible link between fatty acid and ... Chemical synthesis of acyl thioesters of acyl carrier protein with native structure.Proc. Natl. Acad. Sci. USA78198154405444. ... A DNA fragment containing the Pseudomonas aeruginosa fabD (encoding malonyl-coenzyme A [CoA]:acyl carrier protein [ACP] ... Molecular characterization of an Escherichia coli mutant with a temperature-sensitive malonyl coenzyme A:acyl carrier protein ...
acyl-Coenzyme A oxidase 3, pristanoyl. Synonyms: EST-s59, PCOX, pristanoyl-CoA oxidase. Gene nomenclature, locus information, ... OMIM: ACYL-CoA OXIDASE 3, PRISTANOYL; ACOX3*Gene Ontology: Acox3 *Mouse Phenome DB: Acox3 *UCSC: Chr.5:35,583,060-35,613,801(+) ...
... "acyl-Coenzyme A oxidase 1, palmitoyl")*CCDS: 25660, 25660.1, 70354*OMIM: PEROXISOMAL ACYL-CoA OXIDASE DEFICIENCY, ACYL-CoA ... acyl-Coenzyme A oxidase 1, palmitoyl. Synonyms: Acyl-CoA oxidase, AOX, D130055E20Rik. Gene nomenclature, locus information, and ...
Based on automated MP annotations supported by experiments on knockout mouse models. Click on icons to go to all Acadm data for that phenotype. ...
... activity of Acyl coenzyme A:cholesterol acyltransferase 1 in vitro using rat liver microsome.. ...
... cholesterol metabolism in LNCaP and PC-3 cell lines is regulated through two different isoforms of acyl-coenzyme A:Cholesterol ...
Incorporation of [1-14C]Acetate into the Long-Chain-Fatty Acyl-Coenzyme A Esters of Rat Brain in vivo ROBERT W. BONSER; ROBERT ... ROBERT W. BONSER, GEORGE G. LUNT; Incorporation of [1-14C]Acetate into the Long-Chain-Fatty Acyl-Coenzyme A Esters of Rat Brain ...
  • The midway gene encodes a protein similar to mammalian acyl coenzyme A: diacylglycerol acyltransferase (DGAT), which converts diacylglycerol (DAG) into triacylglycerol (TAG). (genetics.org)
  • 1. In the presence of CoA and ATP, human liver microsomes catalyse the incorporation of [ 14 C]oleate or [ 14 C]cholesterol into cholesteryl oleate, thus demonstrating the presence of acyl-coenzyme A-cholesterol acyltransferase (cholesterol acyltransferase) in human liver. (portlandpress.com)
  • 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. (nih.gov)
  • The malonyl-CoA is transferred to the acyl carrier protein (ACP) by malonyl-CoA:ACP acyltransferase (FabD). (asm.org)
  • Concentration required to inhibit 50% activity of Acyl coenzyme A:cholesterol acyltransferase 1 in vitro using rat liver microsome. (nih.gov)
  • We propose that the high degree of acyl specificity of lysophosphatidyl acyltransferase is the blocking step in the synthesis of triacylglycerols using lauroyl CoA or erucoyl CoA. (plantphysiol.org)
  • Increased expression of acyl-coenzyme A: cholesterol acyltransferase-1" by J.-H Kim, S.-M Ee et al. (edu.au)
  • Below are the list of possible Acyl-coenzyme A amino acid N-acyltransferase products. (mybiosource.com)
  • To verify the regulation of acyl- coenzyme A cholesterol acyltransferase 2 (ACAT 2), which is associated with cholesterol metabolism , by saturated fatty acids (SFAs). (bvsalud.org)
  • Identification of crucial residues involved in the catalysis of acyl-coenzyme A:cholesterol acyltransferase. (dartmouth.edu)
  • Biochemical characterization of recombinant acyl coenzyme A:cholesterol acyltransferase expressed in insect Sf9 cell. (dartmouth.edu)
  • Acyl-coenzyme A:cholesterol acyltransferase (ACAT), the enzyme that catalyses the formation of cholesteryl esters, modulates the generation of Aβ through the tight control of the equilibrium between free cholesterol and cholesteryl esters. (elsevier.com)
  • We investigated the mechanism of spontaneous cholesterol efflux induced by acyl-coenzyme A:cholester-ol acyltransferase (ACAT) inhibition, and how an alteration of cholesterol metabolism in macrophages impacts on that in HepG2 cells. (elsevier.com)
  • The diagnosis of short-chain acyl-coenzyme A dehydrogenase deficiency is based on the following: Newborn screening test Genetic testing Urine test The differential diagnosis for short-chain acyl-coenzyme A dehydrogenase deficiency is: ethylmalonic encephalopathy, mitochondrial respiratory chain defects and multiple acyl-CoA dehydrogenase deficiency. (wikipedia.org)
  • In this regard metabolic dysfunction may be associated with an impairment of mitochondrial fatty acid oxidation (mtFAO) which can lead to over accumulation of bioactive lipids such as fatty acyl-CoA species. (uncg.edu)
  • The protein encoded by this gene is a mitochondrial acyl-CoA thioesterase of unknown function. (nih.gov)
  • Medium chain acyl CoA dehydrogenase deficiency is a mitochondrial fatty acid oxidative deficiency disease . (bvsalud.org)
  • Short-chain acyl-CoA dehydrogenase (SCAD) catalyzes the first step in mitochondrial shortchain β-oxidation, and its deficiency is caused by mutations in the ACADS. (elsevier.com)
  • Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. (uniprot.org)
  • 16940157 ). It is unclear if human acyl-coenzyme A thioesterase 6/ACOT6 has an acyl-CoA thioesterase (Probable). (uniprot.org)
  • Small volumes of the liquid components of the Mouse ELISA Kit FOR Acyl-coenzyme A thioesterase 3 might get caught on the lids and on the walls of the vials due to handling and transportation issues. (antibody-antibodies.com)
  • Has acyl-CoA thioesterase activity towards long-chain (C16 and C18) fatty acyl-CoA substrates, with a preference for linoleoyl-CoA and other unsaturated long-chain fatty acid-CoA esters. (nih.gov)
  • Here, we report the characterization of an Arabidopsis cDNA clone encoding for a glyoxysomal acyl-CoA synthetase designated At LACS6. (plantphysiol.org)
  • The cDNA sequence is 2,106 bp long and it encodes a polypeptide of 701 amino acids with a calculated molecular mass of 76,617 D. Analysis of the amino-terminal sequence indicates that acyl-CoA synthetase is synthesized as a larger precursor containing a cleavable amino-terminal presequence so that the mature polypeptide size is 663 amino acids. (plantphysiol.org)
  • Recently reductions of acyl-CoA synthetase (ACS) activity have been identified in skeletal muscle. (uncg.edu)
  • Long chain acyl-CoA synthetase (ACSL) exists as five different isoforms the roles of which are to activate fatty acids to acyl-CoAs in the initial step of fatty acid metabolism (synthesis or oxidation). (uncg.edu)
  • Your search returned 24 Acyl-Coenzyme A Oxidase 1, Palmitoyl ELISA ELISA Kit across 1 supplier. (biocompare.com)
  • These studies report the development of a simple, specific, and highly sensitive fluorometric assay for rat liver peroxisomal fatty acyl-CoA oxidase activity. (wright.edu)
  • After subcellular fractionation of liver homogenates by differential centrifugation, the fatty acyl-CoA oxidase activity distributed like known peroxisomal marker enzymes. (wright.edu)
  • These results demonstrate that the fluorometric assay of fatty acyl-CoA oxidase should be useful in studying the distribution, properties, and subcellular localization of the enzyme, particularly in enzyme sources of low activity or in situations when only small amounts of material are available. (wright.edu)
  • 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)
  • The At LACS6 also shows high amino acid identity to prokaryotic and eukaryotic fatty acyl-CoA synthetases. (plantphysiol.org)
  • Acyl-coenzyme A synthetases (ACSs) catalyze the fundamental, initial reaction in fatty acid metabolism. (elsevier.com)
  • Park, M. V. / Acyl-coenzyme A synthetases . (hw.ac.uk)
  • It is due to defects in the enzyme complex known as medium-chain acyl dehydrogenase ( MCAD ) and reduced activity of this complex. (bionity.com)
  • We prepared a specific antiboty (DM10) against human acyl-conzyme A : cholesterol acyltransnferase (ACAT) and analyzed human tissues by immunohistochemical methods. (nii.ac.jp)
  • Besides the role of ACP in phospholipid ( 6 ) and rhamnolipid ( 3 , 27 ) synthesis, ACPs play central roles in a broad range of other biosynthetic pathways that depend on acyl transfer reactions, including polyketide ( 35 ), nonribosomal peptide ( 1 ), and depsipeptide biosynthesis ( 31 ), as well as in the transacylation of oligosaccharides ( 8 , 11 ) and proteins ( 22 ). (asm.org)
  • Acyl-CoA binding proteins form a highly conserved family of proteins, which bind long chain fatty acid esters with nanomolar affinity. (uwc.ac.za)
  • Our microscopic results point to the role of ACBP as an intermembrane transporter of acyl-CoA and demonstrate the ability of AFM to reveal the remodelling of membranes by surfactants and proteins. (ku.dk)
  • As the acyl group carrier, acyl-CoA can partake in chemical reactions on proteins including histones resulting in mediation of chromatin biology. (stopvivisection.info)
  • Once a fatty acid molecule is "activated" (attached to coenzyme A), a series of four reactions, each catalyzed by a different enzyme, is required to remove each acetyl-coenzyme A molecule. (bionity.com)
  • As the first step involves removal of hydrogen atoms (i.e. an oxidation) from an acyl group, the enzyme complex is known as an acyl dehydrogenase. (bionity.com)
  • These data demonstrated that medium-chain acyl-CoA dehydrogenase accounted for 50% of the activity towards the short-chain substrate, butyryl-CoA, under these conditions, but that antibody against that enzyme could be used to unmask the specific and virtually complete deficiency of short-chain acyl-CoA dehydrogenase in this patient. (elsevier.com)
  • Isothermal titration studies of acetyl-coenzyme A and tobramycin binding to mutant forms of the enzyme indicated that completely conserved C109 does not play any direct role in the binding of either of the substrates, while C70 is directly involved in aminoglycoside binding. (elsevier.com)
  • Thus, the two substrates of this enzyme are (3R)-3-hydroxyacyl-[acyl-carrier-protein] and NADP + , whereas its 3 products are 3-oxoacyl-[acyl-carrier-protein] , NADPH , and H + . (wikipedia.org)
  • The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP + oxidoreductase . (wikipedia.org)
  • Finally, dephospho-CoA is phosphorylated using ATP to coenzyme A by the enzyme dephosphocoenzyme A kinase. (bionity.com)
  • The symptoms of short-chain acyl-CoA dehydrogenase deficiency may be triggered during illnesses such as viral infections. (wikipedia.org)
  • Mutations in the ACADS gene lead to inadequate levels of short-chain acyl-CoA dehydrogenase, which is important for breaking down short-chain fatty acids. (wikipedia.org)
  • In terms of treatment for short-chain acyl-CoA dehydrogenase deficiency, some individuals may not need treatment, while others might follow administration of: Riboflavin Dextrose Anticonvulsants This disorder, epidemiologically speaking, is thought to affect approximately 1 in 50,000 newborns according to Jethva, et al. (wikipedia.org)
  • We have produced AAV5 and AAV8 vectors that express mouse short-chain acyl-CoA dehydrogenase (mSCAD) cDNA under the transcriptional control of the cytomegalovirus-chicken beta-actin hybrid promoter. (umassmed.edu)
  • Medium-chain acyl-CoA dehydrogenase deficiency (MCAD deficiency or MCADD), is a disorder of fatty acid oxidation that impairs the body's ability to break down medium-chain fatty acids into acetyl-CoA. (wikipedia.org)
  • The presence of these acyl carnitines, especially octanoyl-carnitine, is a major diagnostic characteristic of MCAD deficiency. (bionity.com)
  • Her doctor recently called to tell us that her test came back abnormal for medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency. (nih.gov)
  • What are the signs and symptoms of medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency? (nih.gov)
  • Are there factors which can cause a false positive test result for medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency on newborn screen? (nih.gov)
  • The false positive rate for medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency varies between screening programs because of differences in analysis of acylcarnitine (a type of fatty acid). (nih.gov)
  • What follow-up testing can be done to definitively determine if my child has medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency? (nih.gov)
  • ACADM is the only gene known to be associated with medium-chain acyl-coenzyme A dehydrogenase (MCAD) deficiency. (nih.gov)
  • Encephalopathy associated with a reversible splenial lesion in riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency. (harvard.edu)
  • Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency. (harvard.edu)
  • Multi-organ abnormalities and mTORC1 activation in zebrafish model of multiple acyl-CoA dehydrogenase deficiency. (harvard.edu)
  • A case of late onset riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency manifesting as recurrent rhabdomyolysis and acute renal failure. (harvard.edu)
  • Mechanisms underlying metabolic and neural defects in zebrafish and human multiple acyl-CoA dehydrogenase deficiency (MADD). (harvard.edu)
  • Genetic deficiency of short-chain acyl-coenzyme A (CoA) dehydrogenase activity was demonstrated in cultured fibroblasts from a 2-yr-old female whose early postnatal life was complicated by poor feeding, emesis, and failure to thrive. (elsevier.com)
  • Fibroblasts from this patient had 50% of control levels of acyl-CoA dehydrogenase activity towards butyryl-CoA as substrate at a concentration of 50 μM in a fluorometric assay based on the reduction of electron transfer flavoprotein. (elsevier.com)
  • Ten weeks after portal vein injection into 8-week-old mice, AAV8-treated livers contained acyl-CoA dehydrogenase activity (14.3 mU/mg) toward butyryl-CoA, compared with 7.6 mU/mg in mice that received phosphate-buffered saline. (umassmed.edu)
  • Medium-chain acyl-coenzyme A dehydrogenase deficiency is a fatty acid oxidation disorder associated with inborn errors of metabolism . (bionity.com)
  • Androgen-mediated cholesterol metabolism in LNCaP and PC-3 cell lines is regulated through two different isoforms of acyl-coenzyme A:Cholesterol Ac. (nih.gov)
  • CES1 may participate in fatty acyl and cholesterol ester metabolism, and may play a role in maintaining the blood-brain barrier. (thefreedictionary.com)
  • with acyl-carnitine rate of metabolism and other features of the metabolic network that collectively can lead to the finding of biomarkers of acyl-CoA rate of metabolism. (stopvivisection.info)
  • These findings display a strong acyl-CoA profiling method and determine coordinated changes of acyl-CoA rate of metabolism in response to nutritional stress. (stopvivisection.info)
  • Thioester compounds comprising acyl-coenzyme A (acyl-CoA)1 are key metabolites in intermediary rate of metabolism. (stopvivisection.info)
  • Conditions of high excess fat feeding that induce nutritional stress are shown to induce global changes in enzymes in rate of metabolism (19, 20), but a comprehensive assessment of the global alterations in rate of metabolism that remains include possible redesigning of acyl-CoA rate of metabolism remain unfamiliar. (stopvivisection.info)
  • This remodeling could also be associated with acyl-carnitine rate of metabolism that often serves as both a readout of acyl-CoA rate of metabolism and other features of rate of metabolism status. (stopvivisection.info)
  • We apply this method to profile the dynamics of acyl-CoA compounds and corresponding alterations in metabolism across the metabolic network in response to high fat feeding in mice. (mcponline.org)
  • A substantial extent of this metabolic remodeling exhibited correlated changes in acyl-CoA metabolism with acyl-carnitine metabolism and other features of the metabolic network that together can lead to the discovery of biomarkers of acyl-CoA metabolism. (mcponline.org)
  • These findings show a robust acyl-CoA profiling method and identify coordinated changes of acyl-CoA metabolism in response to nutritional stress. (mcponline.org)
  • Short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD), is an autosomal recessive fatty acid oxidation disorder which affects enzymes required to break down a certain group of fats called short chain fatty acids. (wikipedia.org)
  • medical citation needed] Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy (lethargy), poor feeding, and failure to gain weight and grow. (wikipedia.org)
  • Multiple Acyl Coenzyme A Dehydrogenase Deficiency" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Multiple Acyl Coenzyme A Dehydrogenase Deficiency" by people in Harvard Catalyst Profiles by year, and whether "Multiple Acyl Coenzyme A Dehydrogenase Deficiency" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Multiple Acyl Coenzyme A Dehydrogenase Deficiency" by people in Profiles. (harvard.edu)
  • Medium-chain acyl-coenzyme A dehydrogenase deficiency (MCADD) is an inherited metabolic disorder that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). (nih.gov)
  • The initial signs and symptoms of medium-chain acyl-coenzyme A dehydrogenase deficiency (MCADD) typically occur during infancy or early childhood and can include vomiting, lack of energy (lethargy), and low blood sugar (hypoglycemia). (nih.gov)
  • Introduction There is limited understanding of relationships between genotype, phenotype and other conditions contributing to health in neonates with medium-chain acyl-coenzyme A dehydrogenase deficiency (MCADD) identified through newborn screening. (umn.edu)
  • Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. (hmdb.ca)
  • Contribution of the Distal Pocket Residue to the Acyl-Chain-Length Specificity of (R)-Specific Enoyl-Coenzyme A Hydratases from Pseudomonas spp. (asm.org)
  • Of all the phaJ gene products, PhaJ1 Pa shows relatively narrow substrate specificity toward enoyl-CoAs, preferring acyl chain lengths from 4 to 6, whereas PhaJ2 Pa -PhaJ4 Pa shows broad substrate specificity toward enoyl-CoAs, preferring acyl chain lengths from 6 to 12. (asm.org)
  • It is known that acyl-CoA is bound by acyl-CoA binding protein (ACBP) with high affinity and specificity and that ACBP may bind and desorb membrane-bound acyl-CoA via a partly unknown mechanism. (ku.dk)
  • Consequently, considerable effort has been 13063-54-2 supplier spent on developing methods for acyl-CoA and related acyl protein changes measurements (9C17). (stopvivisection.info)
  • May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. (hmdb.ca)
  • 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 ). (plantphysiol.org)
  • A DNA fragment containing the Pseudomonas aeruginosa fabD (encoding malonyl-coenzyme A [CoA]:acyl carrier protein [ACP] transacylase), fabG (encoding β-ketoacyl-ACP reductase), acpP (encoding ACP), and fabF (encoding β-ketoacyl-ACP synthase II) genes was cloned and sequenced. (asm.org)
  • This phenotype suggested that CER4 encoded an alcohol-forming fatty acyl-coenzyme A reductase (FAR). (ubc.ca)
  • The availability of acyl-Coenzyme A (acyl-CoA) thioester compounds affects several cellular functions including autophagy, lipid oxidation and synthesis, and post-translational modifications. (stopvivisection.info)
  • 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. (uniprot.org)
  • PHA synthase polymerizes the ( R )-3-hydroxyalkanoate moiety of ( R )-3-hydroxyacyl coenzyme A (3HA-CoA) into PHA, whereas monomer-supplying enzymes synthesize ( R )-3HA-CoA from various metabolic intermediates. (asm.org)
  • Amino acid sequence similarities were used to assign enzymes into subfamilies, and subfamily assignments were consistent with acyl chain length preference. (elsevier.com)
  • Coenzymes are small compounds that help enzymes trigger chemical reactions that otherwise wouldn't happen on their own. (healthline.com)
  • It seems highly likely that mixtures of isomers with secondary functions on adjacent carbons arise from oxidation catalyzed by P450 enzymes, while mixtures of isomers with alternating group positions are formed by malonate condensation reactions mediated by polyketide synthase or ketoacyl-CoA synthase enzymes, or else by the head-to-head condensation of long-chain acyls. (springer.com)
  • The crystal structure of PhaJ1 Pa was determined at a resolution of 1.7 Å, and subsequent homology modeling of PhaJ1 Pp revealed that in the acyl-chain binding pocket, the amino acid at position 72 was the only difference between the two structures. (asm.org)
  • R )-Specific enoyl-coenzyme A (enoyl-CoA) hydratases (PhaJs) are capable of supplying monomers from fatty acid β-oxidation to polyhydroxyalkanoate (PHA) biosynthesis. (asm.org)
  • Trans -2-enoyl coenzyme A (enoyl-CoA), an intermediate in fatty acid β-oxidation, undergoes stereospecific hydration by the function of PhaJ, resulting in the formation of ( R )-3HA-CoAs. (asm.org)
  • In this in vitro procedure fatty acyl-CoA-dependent H2O2 production was coupled in a peroxidase-catalyzed reaction to the oxidation of scopoletin (6-methoxy-7-hydroxycoumarin), a highly fluorescent compound, to a nonfluorescent product. (wright.edu)
  • Coenzyme A ( CoA , CoASH , or HSCoA ) is a coenzyme , notable for its role in the synthesis and oxidation of fatty acids , and the oxidation of pyruvate in the citric acid cycle . (bionity.com)
  • In an in vitro system, purified ACP functioned as acyl acceptor and H 6 -FabD exhibited malonyl-CoA:ACP transacylase activity. (asm.org)
  • Bacterial fatty acid biosynthesis necessitates a three-carbon precursor, malonyl-coenzyme A (CoA), which is derived from acetyl-CoA by the action of acetyl-CoA carboxylase. (asm.org)
  • A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases. (nih.gov)
  • In PhaJ1 Pp , the replacement of valine with isoleucine at position 72 resulted in an increased preference for enoyl-coenzyme A (CoA) elements with shorter chain lengths. (asm.org)
  • In maize seed and rapeseed, but not palm seed, the kinetics of labeling suggest that lauroyl and erucoyl moieties of the acyl CoAs were incorporated into lysophosphatidic acid but failed to enter into phosphatidic acid and thus the subsequent lipid products. (plantphysiol.org)
  • Active on long chain acyl-CoAs. (nih.gov)
  • Endozepine is an alternative name for the testis-specific isoform of the acyl-CoA binding protein (t-ACBP). (uwc.ac.za)
  • Following incubation with acyl-CoA, it is shown that ACBP is able to reverse the formation of acyl-CoA aggregates and to associate peripherally with acyl-CoA on the membrane surface. (ku.dk)
  • The fatty acids are broken down in stages by the successive removal of molecules of acetyl-coenzyme A, which contains 2 carbon atoms. (bionity.com)
  • Long chain acyl-coenzyme A (acyl-CoA) is a biochemically important amphiphilic molecule that is known to partition strongly into membranes by insertion of the acyl chain. (ku.dk)
  • Moreover, reversed phase ion-paired chromatography coupled to high-resolution MS has also been utilized for short, medium, and long chain acyl-CoA recognition or quantification with the help of stable isotope labeled requirements (10, 13). (stopvivisection.info)
  • The existence of many ACSs suggests that each plays a unique role, directing the acyl-CoA product to a specific metabolic fate. (elsevier.com)
  • Consequently, the acyl-CoA level changes tend to be associated with other metabolic alterations that regulate these critical cellular functions. (mcponline.org)
  • Most cells undergo de novo synthesis of acyl chains. (springer.com)
  • More recently, acyl-ACPs derived from the Fab pathway have been proposed to be the acyl donors for synthesis of acylated homoserine lactones (AHLs) ( 26 , 32 , 40 ). (asm.org)
  • 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 Mg 2+ . (plantphysiol.org)
  • Activation of acyl-coenzyme A:cholesterol acyl-transferase activity by cholesterol is not due to altered mRNA levels in HepG2 cells. (nii.ac.jp)
  • All of this residual activity was inhibited by an antibody against medium-chain acyl-CoA dehydrogenase. (elsevier.com)
  • Here we show a universal method for metabolomics that allows for the detection of an expansive set of acyl-CoA compounds and hundreds of other cellular metabolites. (mcponline.org)
  • Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. (ox.ac.uk)
  • The refolding from denaturing conditions of a small four-helix bundle, the acyl-coenzyme A binding protein, has been investigated by utilizing an array of fast-reaction techniques. (ox.ac.uk)
  • In the presence of erucoyl CoA, the microsomes from all the three species did not produce di- or tri-acyl lipids. (plantphysiol.org)
  • In the presence of lauroyl CoA, only the microsomes from palm, but not those from maize or rapeseed, synthesized di- and tri-acyl lipids. (plantphysiol.org)
  • Reversed phase LC coupled to a triple quadrupole mass spectrometer has been frequently used as for targeted measurements of specific acyl-CoA compounds, because acyl-CoA compounds undergo a common fragmentation, the neutral loss of adenosine diphosphate, which is the basis of multiple reaction monitoring for acyl-CoA measurements. (stopvivisection.info)
  • A molecule of coenzyme A carrying an acetyl group is also referred to as acetyl-CoA . (bionity.com)