Acyl Coenzyme A: S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.Coenzyme ACoenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Sterol O-Acyltransferase: 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.Coenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.Acyltransferases: 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.Diacylglycerol O-Acyltransferase: 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.Retinol O-Fatty-Acyltransferase: An enzyme that catalyzes the acyl group transfer of acyl COENZYME A to RETINOL to generate COENZYME A and a retinyl ester.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.Acyl-CoA Dehydrogenase: 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.Diazepam Binding Inhibitor: 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.Acyl-CoA Oxidase: 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.Organosilicon Compounds: Organic compounds that contain silicon as an integral part of the molecule.Waxes: 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)Fatty Acids: 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)Ricinoleic Acids: Eighteen carbon fatty acids that comprise the great majority of CASTOR OIL, which is from the seed of RICINUS.Ubiquinone: 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.Mycobacteriaceae: A family of gram-positive bacteria found in soil and dairy products and as parasites on animals and man. Several are important pathogens.Acetyl Coenzyme A: 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.Hydroxymethylglutaryl CoA Reductases: Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.Multiple Acyl Coenzyme A Dehydrogenase Deficiency: 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).Fatty Acid Desaturases: 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.Palmitoyl-CoA Hydrolase: 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.Kinetics: The rate dynamics in chemical or physical systems.Carbon-Carbon Ligases: 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.Triazenes: Compounds with three contiguous nitrogen atoms in linear format, H2N-N=NH, and hydrocarbyl derivatives.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Molecular Sequence Data: 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.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Heterocyclic Compounds, 1-Ring: 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.Cholesterol Esters: 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.Sterol Esterase: An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.Penicillium chrysogenum: A mitosporic fungal species used in the production of penicillin.Oxidoreductases: 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)Caprylates: 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.Glycerol-3-Phosphate O-Acyltransferase: 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.Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.EstersAmino Acid Sequence: 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.Coenzyme A-Transferases: 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.Esterification: 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.CobamidesOleic Acids: A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.Carboxylic Ester Hydrolases: Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.Escherichia coli: 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.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Mesna: A sulfhydryl compound used to prevent urothelial toxicity by inactivating metabolites from ANTINEOPLASTIC AGENTS, such as IFOSFAMIDE or CYCLOPHOSPHAMIDE.Oleic Acid: 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)Acylation: The addition of an organic acid radical into a molecule.Cloning, Molecular: 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.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.Pantothenic Acid: 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.Microbodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.Pantetheine: An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.Bacterial Proteins: Proteins found in any species of bacterium.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Oxidation-Reduction: 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).Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.NAD: 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)Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Genes, Bacterial: The functional hereditary units of BACTERIA.Molecular Weight: The sum of the weight of all the atoms in a molecule.TriglyceridesMutation: 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.Euryarchaeota: 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.Propanediol Dehydratase: An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.Malonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.NADP: 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)Acetate-CoA Ligase: 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.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Methanosarcina barkeri: A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Mevalonic AcidHydroxymethylglutaryl-CoA Reductase Inhibitors: Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.Riboflavin: 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.Methanobacterium: 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.Lovastatin: 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.Phosphatidylcholines: 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.Macrophages: 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.)Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Molecular 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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Phospholipids: 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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Cells, Cultured: 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.Pyridoxal Phosphate: 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).Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent: Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.Methylmalonyl-CoA Mutase: 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.Magnetic Resonance Spectroscopy: 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).Methane: 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)Structure-Activity Relationship: 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, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Hydrogen-Ion Concentration: 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)Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Oxo-Acid-Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.Molecular Conformation: The characteristic three-dimensional shape of a molecule.Corrinoids: Cyclic TETRAPYRROLES based on the corrin skeleton.Simvastatin: 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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Vitamin B 12: 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.Phosphate Acetyltransferase: 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.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Fatty Acid Synthase, Type II: 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.Sterols: 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)Flavin-Adenine Dinucleotide: A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)Thiolester HydrolasesChromatography, Thin Layer: 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)Glutamate Dehydrogenase: 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.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.Acyl-Carrier Protein S-Malonyltransferase: 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.MercaptoethanolProtein Binding: 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.Methanosarcina: 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.Hydroxymethylglutaryl-CoA Synthase: 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.Phosphatidylethanolamines: 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.Methyltransferases: 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 2.1.1.3-Oxoacyl-(Acyl-Carrier-Protein) Synthase: 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.Ethanolamine Ammonia-Lyase: An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.Apoenzymes: 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.Membrane Lipids: 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.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Temperature: 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.Protein Conformation: 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).Palmitic Acids: A group of 16-carbon fatty acids that contain no double bonds.Alcohol Dehydrogenase: 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.Lipid Bilayers: Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Spectrophotometry, Ultraviolet: 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)GlutaratesRecombinant Proteins: Proteins prepared by recombinant DNA technology.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Lipids: 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)Calorimetry, Differential Scanning: 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.Clostridium: 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.Succinate-CoA Ligases: 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.-.MalonatesFatty Acids, Unsaturated: FATTY ACIDS in which the carbon chain contains one or more double or triple carbon-carbon bonds.Acetyl-CoA C-Acetyltransferase: 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.Stereoisomerism: 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)Carboxy-Lyases: 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.Propionates: Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.Mitochondria: 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)Propylene Glycol: A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.Xanthobacter: 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)Acetyl-CoA Carboxylase: 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.Methanobacteriaceae: 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.Heptanoic Acids: 7-carbon saturated monocarboxylic acids.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Multienzyme Complexes: 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.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Flavin Mononucleotide: 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.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Acetyl-CoA C-Acyltransferase: 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.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Lipid A: Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.Intramolecular Transferases: 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.Sulfhydryl Compounds: Compounds containing the -SH radical.Enzymes and Coenzymes: Biological catalysts and their cofactors.Hydro-Lyases: Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.Succinates: 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.Parabens: 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)Methanol: 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.Glycerophosphates: Any salt or ester of glycerophosphoric acid.DimethylaminesPolyketide Synthases: Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.Pterins: Compounds based on 2-amino-4-hydroxypteridine.Streptomyces: 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.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.Sequence Alignment: 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.Archaeal Proteins: Proteins found in any species of archaeon.Sphingomyelins: 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.Enzyme Stability: 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.Dihydroxyacetone Phosphate: An important intermediate in lipid biosynthesis and in glycolysis.Adenosine Triphosphate: 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
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.
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.. ...
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 ...
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
PAC275Hu01, ACOX; PALMCOX; SCOX; Peroxisomal Acyl-Coenzyme A Oxidase 1; Straight-chain acyl-CoA oxidase | Products for research use only!
The mission of the Womens Finance CRG is to provide a safe space for women to share their financial knowledge, research topics of interest, set financial goals, and become financially independent and well informed. The Womens Finance CRG meets on the third Thursday of every month and is sponsored by the Office of Equality and Diversity, the Womens and Gender Studies program, and CoAS. ...
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 ...
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. ...
Methylmalonyl Coenzyme A mutase Lysates available through Novus Biologicals. Browse our Methylmalonyl Coenzyme A mutase Lysate catalog backed by our Guarantee+.
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. ...
Shop Mycocerosic acid synthase ELISA Kit, Recombinant Protein and Mycocerosic acid synthase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
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
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 ...
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. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis.
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. ...
Formula: C14H18N2O8MW: 342. 31CAS: 23646-68-6MDL: MFCD01457171TNP: TNP004214-NITROPHENYL PALMITATE (4-NITROPHENYL HEXADECANOATE; LogP: 2....
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?
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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Acyl-CoA binding domain containing 3 (ACBD3) is involved in the maintenance of Golgi structure and function through its interaction with the integral membrane protein. However, the clinical significance and biological role of ACBD3 in breast cancer remain unclear. Herein, we found that the mRNA and …
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). ...
ACADSB 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. Defects in ACADSB are the cause of short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD); also known as 2-methylbutyryl-CoA dehydrogenase deficiency or 2- methylbutyryl glycinuria. SBCADD is an autosomal recessive disorder and consists of a defect in catabolism of L-isoleucine which is characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine. Affected individuals have seizures and psychomotor delay as the main clinical features. Belongs to the acyl-CoA dehydrogenase family. Note: This description may include information from UniProtKB ...
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 ... 1998). "Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes". J. Biol. ... 2004). "Overexpression of human diacylglycerol acyltransferase 1, acyl-coa:cholesterol acyltransferase 1, or acyl-CoA: ...
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 ... 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 ... As short-chain acyl-CoA dehydrogenase is involved in beta-oxidation, a deficiency in this enzyme is marked by an increased ...
This acyl-Coenzyme A dehydrogenase is specific to long-chain and very-long-chain fatty acids. A deficiency in this gene product ... "Very Long-Chain Acyl-Coenzyme a Dehydrogenase Deficiency". 1993. PMID 20301763. GeneReviews/NCBI/NIH/UW entry on Very long- ... Mutations in the ACADVL are associated with very long-chain acyl-coenzyme A dehydrogenase deficiency. The protein encoded by ... ACADVL is linked with very long-chain acyl-coenzyme A dehydrogenase deficiency (VLCADD), which has many symptoms, and typically ...
... (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ... Medium-chain acyl-coenzyme A dehydrogenase deficiency can be caused by mutations in the ACADM gene. More than 30 ACADM gene ... The acyl-coenzyme A dehydrogenase for medium-chain fatty acids (ACADM) enzyme is essential for converting these particular ... 1993). "Medium-Chain Acyl-Coenzyme A Dehydrogenase Deficiency". PMID 20301597. Gregersen N, Andresen BS, Bross P, Winter V, ...
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. Molecular and ... In enzymology, a retinol O-fatty-acyltransferase (EC 2.3.1.76) is an enzyme that catalyzes the chemical reaction acyl-CoA + ... The systematic name of this enzyme class is acyl-CoA:retinol O-acyltransferase. Other names in common use include retinol ...
Peroxisomal acyl-coenzyme A oxidase 3 is an enzyme that in humans is encoded by the ACOX3 gene. Acyl-Coenzyme A oxidase 3 also ... "Entrez Gene: ACOX3 acyl-Coenzyme A oxidase 3, pristanoyl". Human ACOX3 genome location and ACOX3 gene details page in the UCSC ... 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: ...
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: ...
... acyl-Coenzyme A binding domain containing 3". Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y (November 2001 ...
"Entrez Gene: ACAD9 acyl-Coenzyme A dehydrogenase family, member 9". Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, ... Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T (Jun 1995). "Purification of human very-long-chain acyl-coenzyme A ... Acyl-CoA dehydrogenase family member 9, mitochondrial is an enzyme that in humans is encoded by the ACAD9 gene. The ACAD9 gene ... Ensenauer R, He M, Willard JM, Goetzman ES, Corydon TJ, Vandahl BB, Mohsen AW, Isaya G, Vockley J (Sep 2005). "Human acyl-CoA ...
"Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8". Battaile KP, Nguyen TV, Vockley J, Kim JJ (2004). " ... The protein encoded by ACAD8 is a mitochondrial protein belongs to the acyl-CoA dehydrogenase family of enzymes, which function ... ACAD8 functions as a homotetramer and has an overall structure is similar to other acyl-CoA dehydrogenases. The functional ... and short-chain acyl-CoA dehydrogenases". The Journal of Biological Chemistry. 279 (16): 16526-34. doi:10.1074/jbc.M400034200. ...
Glick BS, Rothman JE (1987). "Possible role for fatty acyl-coenzyme A in intracellular protein transport". Nature. 326 (6110): ...
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 ... Coenzyme A, and free fatty acids. Recent studies have shown that Acyl-CoA esters have many more functions than simply an energy ...
"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". ...
Medium-chain acyl-coenzyme A dehydrogenase deficiency (often shortened to MCADD.) Disorders of porphyrin metabolism E.g., acute ...
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- ...
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 ... acyl-Coenzyme A: cholesterol acyltransferase) 1". Template:PBB ng Further readi. ... Acyl-CoA:cholesterol acyltransferase GRCh38: Ensembl release 89: ENSG00000057252 - Ensembl, May 2017 GRCm38: Ensembl release 89 ...
... 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 ...
Abbreviations: ACP - Acyl carrier protein, CoA - Coenzyme A, NADP - Nicotinamide adenine dinucleotide phosphate. Note that ... This system is distinct from the branched-chain fatty acid synthetase that utilizes short-chain acyl-CoA esters as primers. α- ... and branch-chain fatty acid synthase is substrate specificity of the enzyme that catalyzes the reaction of acyl-CoA to acyl-ACP ... to interact with the saturated fatty acyl-CoA chain, forming a double bond and two molecules of water, H2O. Two electrons come ...
... 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 ... The liberated carnitine is shuttled back to the cytosol, as an acyl-CoA is shuttled into the matrix. Beta oxidation, in the ...
... acyl-CoA acyltransferase. This enzyme participates in ether lipid metabolism. Waku K, Lands WE (1968). "Acyl coenzyme A:1- ... In enzymology, a plasmalogen synthase (EC 2.3.1.25) is an enzyme that catalyzes the chemical reaction acyl-CoA + 1-O-alk-1-enyl ... The systematic name of this enzyme class is acyl-CoA:1-O-alk-1-enyl-glycero-3-phosphocholine 2-O-acyltransferase. Other names ... the two substrates of this enzyme are acyl-CoA and 1-O-alk-1-enyl-glycero-3-phosphocholine, whereas its two products are CoA ...
Enoyl-acyl carrier protein reductase/Enoyl ACP reductase. *7-Dehydrocholesterol reductase. *Biliverdin reductase ...
We recently identified acyl coenzyme A-binding proteins (ACBP)/diazepam binding inhibitor (DBI) being a book hunger aspect: a ... We recently identified acyl coenzyme A-binding proteins (ACBP)/diazepam binding inhibitor (DBI) being a book hunger aspect: a ...
Pantothenic acid is a water-soluble vitamin, which is a component of coenzyme A (CoA) and acyl-carrier proteins. Pantothenic ...
1996) Ethylmalonic aciduria is associated with an amino acid variant of short chain acyl-coenzyme A dehydrogenase. Pediatr Res ... Free and acyl carnitines were detected and measured by setting the instrument to detect precursors of m/z (mass/charge ratio) ... 1988) The use of phenylpropionic acid as a loading test for medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis ... 1991) Prevalence of K329E mutation in medium-chain acyl-CoA dehydrogenase gene determined from Guthrie cards. Lancet 338:552- ...
Acyl Coenzyme A binding domain containing 1. *Acyl coenzyme A binding protein ... Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA ...
Short-chain acyl-coenzyme A dehydrogenase deficiency (SCADD), also called ACADS deficiency and SCAD deficiency, is an autosomal ... 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. Leydiker, K. B.; Neidich, J. A.; Lorey, F.; Barr, E. M ... Medium-chain acyl-CoA dehydrogenase deficiency, often known as MCAD deficiency or MCADD, is a disorder of fatty acid oxidation ...
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 ...
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" ...
Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs (By ... Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. ... Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. ... Peroxisomal acyl-coenzyme A oxidase 1Add BLAST. 661. Amino acid ... IPR029320 Acyl-CoA_ox_N. IPR006091 Acyl-CoA_Oxase/DH_cen-dom. IPR012258 Acyl-CoA_oxidase. IPR002655 Acyl-CoA_oxidase_C. ...
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, ...
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. ...
Inhibition of acyl coenzyme A:cholesterol acyltransferase (ACAT) activity in rat liver microsome. ...
Acyl-Coenzyme A:Cholesterol O-Transferase explanation free. What is Acyl-Coenzyme A:Cholesterol O-Transferase? Meaning of Acyl- ... Coenzyme A:Cholesterol O-Transferase medical term. What does Acyl-Coenzyme A:Cholesterol O-Transferase mean? ... Looking for online definition of Acyl-Coenzyme A:Cholesterol O-Transferase in the Medical Dictionary? ... Acyl-Coenzyme A:Cholesterol O-Transferase , definition of Acyl-Coenzyme A:Cholesterol O-Transferase by Medical dictionary https ...
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 ...
  • Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs (By similarity). (uniprot.org)
  • 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)
  • The acyl groups in RL are primarily β-hydroxydecanoyl, and in vitro, RhlA has a greater affinity for 10-carbon substrates, illustrating that RhlA functions as a molecular ruler that selectively extracts 10-carbon intermediates from FASII. (asm.org)
  • This reduced coenzyme is then a substrate for any of the reductases in the cell that need to reduce their substrates (Pollak et al. (newworldencyclopedia.org)
  • 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)
  • 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)
  • Consequently, the acyl-CoA level changes tend to be associated with other metabolic alterations that regulate these critical cellular functions. (mcponline.org)
  • 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)
  • The availability of acyl-Coenzyme A (acyl-CoA) thioester compounds affects numerous cellular functions including autophagy, lipid oxidation and synthesis, and post-translational modifications. (mcponline.org)
  • 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)
  • medical citation needed] Short-chain acyl-coenzyme A dehydrogenase deficiency affected infants will have vomiting, low blood sugar, a lack of energy (lethargy), poor feeding, and failure to gain weight and grow. (wikipedia.org)
  • The 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)
  • Here, 13 drugs with a carboxylic acid moiety were incubated with human liver microsomes to produce acyl glucuronide conjugates for the determination of acyl glucuronide half-lives by acyl migration and with HepaRG cells to monitor the formation of acyl CoA conjugates, their further conjugate metabolites, and trans-acylation products with glutathione. (bireme.br)
  • Contribution of the Distal Pocket Residue to the Acyl-Chain-Length Specificity of (R)-Specific Enoyl-Coenzyme A Hydratases from Pseudomonas spp. (asm.org)
  • 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)
  • Many carboxylic acid-containing drugs are associated with idiosyncratic drug toxicity (IDT), which may be caused by reactive acyl glucuronide metabolites. (bireme.br)
  • On the basis of the results, the short relative half-life of the acyl glucuronide (high acyl migration rate), high daily dose and detection of acyl CoA conjugates, or further metabolites derived from acyl CoA together seem to indicate that carboxylic acid-containing drugs have a higher probability to cause drug-induced liver injury (DILI). (bireme.br)
  • Active on long chain acyl-CoAs. (nih.gov)
  • 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)
  • Long-chain acyl-CoA levels were higher in perirenal than in epididymal preadipocytes and isolated fat cells. (biomedsearch.com)
  • 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)
  • 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)
  • 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)