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.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.Coenzyme APyruvate Carboxylase: A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.Epoxide Hydrolases: Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively.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.ATP Citrate (pro-S)-Lyase: An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATE. This reaction represents an important step in fatty acid biosynthesis. This enzyme was formerly listed as EC 4.1.3.8.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.Ligases: A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.Lactase-Phlorizin Hydrolase: The multifunctional protein that contains two enzyme domains. The first domain (EC 3.2.1.62) hydrolyzes glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. The second domain (EC 3.2.1.108) hydrolyzes LACTOSE and is found in the intestinal brush border membrane. Loss of activity for this enzyme in humans results in LACTOSE INTOLERANCE.Biotin: A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.Hydrolases: Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.Acetylcarnitine: An acetic acid ester of CARNITINE that facilitates movement of ACETYL COA into the matrices of mammalian MITOCHONDRIA during the oxidation of FATTY ACIDS.Acetyl-CoA Hydrolase: An enzyme that catalyzes reversibly the hydrolysis of acetyl-CoA to yield CoA and acetate. The enzyme is involved in the oxidation of fatty acids. EC 3.1.2.1.Adenosylhomocysteinase: An enzyme which catalyzes the catabolism of S-ADENOSYLHOMOCYSTEINE to ADENOSINE and HOMOCYSTEINE. It may play a role in regulating the concentration of intracellular adenosylhomocysteine.Magnesium Compounds: Inorganic compounds that contain magnesium as an integral part of the molecule.gamma-Glutamyl Hydrolase: Catalyzes the hydrolysis of pteroylpolyglutamic acids in gamma linkage to pterolylmonoglutamic acid and free glutamic acid. EC 3.4.19.9.Malonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.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.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.Rhizobium etli: A species of gram-negative bacteria and nitrogen innoculant of PHASEOLUS VULGARIS.AmidohydrolasesCarboxylic Ester Hydrolases: Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.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)Kinetics: The rate dynamics in chemical or physical systems.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.Acetylesterase: An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.CitratesMevalonic AcidAcetylation: Formation of an acetyl derivative. (Stedman, 25th ed)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.Thiolester HydrolasesCarbon Isotopes: Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.AMP-Activated Protein Kinases: Intracellular signaling protein kinases that play a signaling role in the regulation of cellular energy metabolism. Their activity largely depends upon the concentration of cellular AMP which is increased under conditions of low energy or metabolic stress. AMP-activated protein kinases modify enzymes involved in LIPID METABOLISM, which in turn provide substrates needed to convert AMP into ATP.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.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.Citric Acid Cycle: A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.Allophanate Hydrolase: An enzyme that catalyzes the hydrolysis of allophanic acid to two molecules of ammonia plus two molecules of "active carbon dioxide". EC 3.5.1.54.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Amino 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.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.Organophosphates: Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.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.Glycoside HydrolasesMitochondria, Liver: Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Carbon Radioisotopes: Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.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.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.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Adipose Tissue: Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.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.Rats, Inbred Strains: Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.Dietary Carbohydrates: Carbohydrates present in food comprising digestible sugars and starches and indigestible cellulose and other dietary fibers. The former are the major source of energy. The sugars are in beet and cane sugar, fruits, honey, sweet corn, corn syrup, milk and milk products, etc.; the starches are in cereal grains, legumes (FABACEAE), tubers, etc. (From Claudio & Lagua, Nutrition and Diet Therapy Dictionary, 3d ed, p32, p277)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)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).Leukotriene A4: (2S-(2 alpha,3 beta(1E,3E,5Z,8Z)))-3-(1,3,5,8-Tetradecatetraenyl)oxiranebutanoic acid. An unstable allylic epoxide, formed from the immediate precursor 5-HPETE via the stereospecific removal of a proton at C-10 and dehydration. Its biological actions are determined primarily by its metabolites, i.e., LEUKOTRIENE B4 and cysteinyl-leukotrienes. Alternatively, leukotriene A4 is converted into LEUKOTRIENE C4 by glutathione-S-transferase or into 5,6-di-HETE by the epoxide-hydrolase. (From Dictionary of Prostaglandins and Related Compounds, 1990)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.N-Acetylmuramoyl-L-alanine Amidase: An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Sterol Esterase: An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.Ubiquitin Thiolesterase: A thioester hydrolase which acts on esters formed between thiols such as DITHIOTHREITOL or GLUTATHIONE and the C-terminal glycine residue of UBIQUITIN.Hydroxymethylglutaryl CoA Reductases: Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.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.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.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Acetate Kinase: An enzyme that catalyzes reversibly the phosphorylation of acetate in the presence of a divalent cation and ATP with the formation of acetylphosphate and ADP. It is important in the glycolysis process. EC 2.7.2.1.Insulin: A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Bacterial Proteins: Proteins found in any species of bacterium.Endocannabinoids: Fatty acid derivatives that have specificity for CANNABINOID RECEPTORS. They are structurally distinct from CANNABINOIDS and were originally discovered as a group of endogenous CANNABINOID RECEPTOR AGONISTS.Dietary Fats: Fats present in food, especially in animal products such as meat, meat products, butter, ghee. They are present in lower amounts in nuts, seeds, and avocados.Polyunsaturated Alkamides: Amides composed of unsaturated aliphatic FATTY ACIDS linked with AMINES by an amide bond. They are most prominent in ASTERACEAE; PIPERACEAE; and RUTACEAE; and also found in ARISTOLOCHIACEAE; BRASSICACEAE; CONVOLVULACEAE; EUPHORBIACEAE; MENISPERMACEAE; POACEAE; and SOLANACEAE. They are recognized by their pungent taste and for causing numbing and salivation.Energy Metabolism: The chemical reactions involved in the production and utilization of various forms of energy in cells.Carbamates: Derivatives of carbamic acid, H2NC(=O)OH. Included under this heading are N-substituted and O-substituted carbamic acids. In general carbamate esters are referred to as urethanes, and polymers that include repeating units of carbamate are referred to as POLYURETHANES. Note however that polyurethanes are derived from the polymerization of ISOCYANATES and the singular term URETHANE refers to the ethyl ester of carbamic acid.Monoacylglycerol Lipases: An enzyme that catalyzes the hydrolysis of glycerol monoesters of long-chain fatty acids EC 3.1.1.23.Phenylacetates: Derivatives of phenylacetic acid. Included under this heading are a variety of acid forms, salts, esters, and amides that contain the benzeneacetic acid structure. Note that this class of compounds should not be confused with derivatives of phenyl acetate, which contain the PHENOL ester of ACETIC ACID.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.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)Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.EsterasesModels, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Xylans: Polysaccharides consisting of xylose units.Carboxylesterase: Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.S-Adenosylhomocysteine: 5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions.Astemizole: Antihistamine drug now withdrawn from the market in many countries because of rare but potentially fatal side effects.Muscle, Skeletal: A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Pyrophosphatases: A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-.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.EstersEpoxy Compounds: Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Aminopeptidases: A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.Cannabinoid Receptor Modulators: Compounds that interact with and modulate the activity of CANNABINOID RECEPTORS.Arachidonic AcidsMolecular Weight: The sum of the weight of all the atoms in a molecule.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.NitrophenolsParaoxon: An organophosphate cholinesterase inhibitor that is used as a pesticide.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.8,11,14-Eicosatrienoic Acid: A 20-carbon-chain fatty acid, unsaturated at positions 8, 11, and 14. It differs from arachidonic acid, 5,8,11,14-eicosatetraenoic acid, only at position 5.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.Xylosidases: A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.Mutation: 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.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.beta-Glucosidase: An exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of GLUCOSE.Cellulase: An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Endo-1,4-beta Xylanases: Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.Lactase: An enzyme which catalyzes the hydrolysis of LACTOSE to D-GALACTOSE and D-GLUCOSE. Defects in the enzyme cause LACTOSE INTOLERANCE.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Acid Anhydride Hydrolases: A group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.Genes, Bacterial: The functional hereditary units of BACTERIA.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Adipates: Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.Tubercidin: An antibiotic purine ribonucleoside that readily substitutes for adenosine in the biological system, but its incorporation into DNA and RNA has an inhibitory effect on the metabolism of these nucleic acids.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.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Lipase: An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.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.Pantetheine: An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Protein 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.Benzoates: Derivatives of BENZOIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxybenzene structure.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)N-Glycosyl Hydrolases: A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars.Adamantane: A tricyclo bridged hydrocarbon.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Microsomes: Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)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).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.Lauric Acids: 12-Carbon saturated monocarboxylic acids.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Phenylmethylsulfonyl Fluoride: An enzyme inhibitor that inactivates IRC-50 arvin, subtilisin, and the fatty acid synthetase complex.Chromatography, 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)Acylation: The addition of an organic acid radical into a molecule.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)Hydroxybutyrates: Salts and esters of hydroxybutyric acid.Organophosphorus Compounds: Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Enzyme Assays: Methods used to measure the relative activity of a specific enzyme or its concentration in solution. Typically an enzyme substrate is added to a buffer solution containing enzyme and the rate of conversion of substrate to product is measured under controlled conditions. Many classical enzymatic assay methods involve the use of synthetic colorimetric substrates and measuring the reaction rates using a spectrophotometer.Amylopectin: A highly branched glucan in starch.Solubility: The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Palmitic Acids: A group of 16-carbon fatty acids that contain no double bonds.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Subcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Hydroxymercuribenzoates: Hydroxylated benzoic acid derivatives that contain mercury. Some of these are used as sulfhydryl reagents in biochemical studies.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.Receptor, Cannabinoid, CB1: A subclass of cannabinoid receptor found primarily on central and peripheral NEURONS where it may play a role modulating NEUROTRANSMITTER release.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Carboxylic Acids: Organic compounds containing the carboxy group (-COOH). This group of compounds includes amino acids and fatty acids. Carboxylic acids can be saturated, unsaturated, or aromatic.MalonatesAldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.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.Clofibrate: A fibric acid derivative used in the treatment of HYPERLIPOPROTEINEMIA TYPE III and severe HYPERTRIGLYCERIDEMIA. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986)Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Butyrates: Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.Crotonates: Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.Isoflurophate: A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Cellulose: A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.Biodegradation, Environmental: Elimination of ENVIRONMENTAL POLLUTANTS; PESTICIDES and other waste using living organisms, usually involving intervention of environmental or sanitation engineers.Cellulases: A family of glycosidases that hydrolyse crystalline CELLULOSE into soluble sugar molecules. Within this family there are a variety of enzyme subtypes with differing substrate specificities that must work together to bring about complete cellulose hydrolysis. They are found in structures called CELLULOSOMES.Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)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.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Trypanosoma vivax: An active blood parasite that is present in practically all domestic animals in Africa, the West Indies, and parts of Central and South America. In Africa, the insect vector is the tsetse fly. In other countries, infection is by mechanical means indicating that the parasites have been introduced to these countries and have been able to maintain themselves in spite of the lack of a suitable intermediate host. It is a cause of nagana, the severity of which depends on the species affected.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.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.-.Acetic Acid: Product of the oxidation of ethanol and of the destructive distillation of wood. It is used locally, occasionally internally, as a counterirritant and also as a reagent. (Stedman, 26th ed)Glycerides: GLYCEROL esterified with FATTY ACIDS.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.Enoyl-CoA Hydratase: An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.Aspergillus niger: An imperfect fungus causing smut or black mold of several fruits, vegetables, etc.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.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.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Butyrylcholinesterase: An aspect of cholinesterase (EC 3.1.1.8).Chromatography: Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.Histone Acetyltransferases: Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.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.Pyruvate Dehydrogenase Complex: A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Crystallization: The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Cell Wall: The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.
Porcine kidney microsomal cysteine S-conjugate N-acetyltransferase-catalyzed N-acetylation of haloalkene-derived cysteine S-conjugates. (1/30)
N-Acetylation of xenobiotic-derived cysteine S-conjugates is a key step in the mercapturic acid pathway. The aim of this study was to investigate the N-acetylation of haloalkene-derived S-haloalkyl and S-haloalkenyl cysteine S-conjugates by porcine kidney cysteine S-conjugate N-acetyltransferase (NAcT). A radioactive assay for the quantification of NAcT activity was developed as a new method for partial purification of the enzyme, which was necessitated by the substantial loss of activity during the immunoaffinity chromatography method. 3-[(3-Cholamidopropyl)dimethylammonio]-1-propane-sulfonate, rather than N,N-bis[3-gluconamidopropyl]deoxycholamide, was used to solubilize the NAcT from porcine kidney microsomes in the revised procedure. The partially purified NAcT was free of detectable aminoacylase activity. Although low acetyl-coenzyme A hydrolase activity was observed, its effect on the assay was minimized by addition of excess acetyl-coenzyme A in the NAcT assay mixture. Attempts to separate the residual hydrolase activity from NAcT by different chromatographic procedures were either unsuccessful or lead to inactivation of NAcT. Most of the cysteine S-conjugates studied were N-acetylated by NAcT. Although the apparent K(m) values for the cysteine S-conjugates studied differed by a factor of approximately 2.5 (124-302 microM), a greater than 15-fold difference in the apparent V(max) (0.75-15.6 nmol/h) and V(max)/K(m) (0.008-0.126 x 10(-3) l h(-1)) values was observed. These data show that a range of haloalkene-derived cysteine S-conjugates serve as substrates for pig kidney NAcT. The significant differences in cytotoxicity of these conjugates may be a result of more variable deacetylation rates of the corresponding mercapturates. (+info)Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase. (2/30)
A cytosolic acetyl-CoA hydrolase (CACH) was purified from rat liver to homogeneity by a new method using Triton X-100 as a stabilizer. We digested the purified enzyme with an endopeptidase and determined the N-terminal amino-acid sequences of the two proteolytic fragments. From the sequence data, we designed probes for RT-PCR, and amplified CACH cDNA from rat liver mRNA. The CACH cDNA contains a 1668-bp ORF encoding a protein of 556 amino-acid residues (62 017 Da). Recombinant expression of the cDNA in insect cells resulted in overproduction of functional acetyl-CoA hydrolase with comparable acyl-CoA chain-length specificity and Michaelis constant for acetyl-CoA to those of the native CACH. Database searching shows no homology to other known proteins, but reveals high similarities to two mouse expressed sequence tags (91% and 93% homology) and human mRNA for KIAA0707 hypothetical protein (50% homology) of unknown function. (+info)Production of acetate in the liver and its utilization in peripheral tissues. (3/30)
In experimental rat liver perfusion we observed net production of free acetate accompanied by accelerated ketogenesis with long-chain fatty acids. Mitochondrial acetyl-CoA hydrolase, responsible for the production of free acetate, was found to be inhibited by the free form of CoA in a competitive manner and activated by reduced nicotinamide adenine dinucleotide (NADH). The conditions under which the ketogenesis was accelerated favored activation of the hydrolase by dropping free CoA and elevating NADH levels. Free acetate was barely metabolized in the liver because of low affinity, high K(m), of acetyl coenzyme A (acetyl-CoA) synthetase for acetate. Therefore, infused ethanol was oxidized only to acetate, which was entirely excreted into the perfusate. The acetyl-CoA synthetase in the heart mitochondria was much lower in K(m) than it was in the liver, thus the heart mitochondria was capable of oxidizing free acetate as fast as other respiratory substrates, such as succinate. These results indicate that rat liver produces free acetate as a byproduct of ketogenesis and may supply free acetate, as in the case of ketone bodies, to extrahepatic tissues as fuel. (+info)Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression. (4/30)
A cytosolic acetyl-CoA hydrolase (CACH) cDNA has been isolated from mouse liver cDNA library and sequenced. Recombinant expression of the cDNA in insect cells resulted in overproduction of active acetyl-CoA hydrolyzing enzyme protein. The mouse CACH cDNA encoded a 556-amino-acid sequence that was 93.5% identical to rat CACH, suggesting a conserved role for this enzyme in the mammalian liver. Database searching shows no homology to other known proteins, but reveals homological cDNA sequences showing two single-nucleotide polymorphisms (SNPs) in the CACH coding region. The discovery of mouse CACH cDNA is an important step towards genetic studies on the functional analysis of this enzyme by gene-knockout and transgenic approaches. (+info)Functional characterization and localization of acetyl-CoA hydrolase, Ach1p, in Saccharomyces cerevisiae. (5/30)
Acetyl-CoA hydrolase (Ach1p), catalyzing the hydrolysis of acetyl-CoA, is presumably involved in regulating intracellular acetyl-CoA or CoASH pools; however, its intracellular functions and distribution remain to be established. Using site-directed mutagenesis analysis, we demonstrated that the enzymatic activity of Ach1p is dependent upon its putative acetyl-CoA binding sites. The ach1 mutant causes a growth defect in acetate but not in other non-fermentable carbon sources, suggesting that Ach1p is not involved in mitochondrial biogenesis. Overexpression of Ach1p, but not constructs containing acetyl-CoA binding site mutations, in ach1-1 complemented the defect of acetate utilization. By subcellular fractionation, most of the Ach1p in yeast was distributed with mitochondria and little Ach1p in the cytoplasm. By immunofluorescence microscopy, we show that Ach1p and acetyl-CoA binding site-mutated constructs, but not its N-terminal deleted construct, are localized in mitochondria. Moreover, the onset of pseudohyphal development in homozygote ach1-1 diploids was abolished. We infer that Ach1p may be involved in a novel acetyl-CoA biogenesis and/or acetate utilization in mitochondria and thereby indirectly affect pseudohyphal development in yeast. (+info)Physiological difference between dietary obesity-susceptible and obesity-resistant Sprague Dawley rats in response to moderate high fat diet. (6/30)
The primary aim of the present study was to define central and peripheral physiological differences between dietary obesity-susceptible (DOS) and obesity-resistant (DOR) outbred Sprague Dawley (SD) rats when given a moderate high fat diet containing 32.34% of energy as a fat. After a 9-week feeding period, the DOS-SD rats consumed significantly more feed (11.1%) and had higher abdominal (39.9%) and epididymal (27.5%) fat pads than the DOR-SD rats. In addition, serum leptin and insulin levels were significantly increased in the DOS-SD rats compared with those in the DOR-SD rats. However, we did not observe significant differences in serum triglyceride, cholesterol and glucose. No differences in hypothalamic OB-Ra and Rb mRNA expressions were found between the two groups. In contrast, arcuate NPY immunohistochemical expression was much higher in the DOS-SD rats than in the DOR-SD rats, though NPY expression in the supraoptic and paraventricular nuclei was not different between the two phenotypes. In peripheral tissues, the DOS-SD rats showed noticeably increased acetyl CoA carboxylase (ACC) mRNA expression in the liver, not epididymal fat. However, Western blot of peroxisomal proliferator activated factor gamma (PPAR gamma) in the liver and epididymal fat was not different between the two phenotypes of SD rats. It was concluded that different body weight phenotypes within outbred SD population responded differently to the development of dietary induced obesity via altered anabolic features in the hypothalamus and liver. (+info)An acetate-sensitive mutant of Neurospora crassa deficient in acetyl-CoA hydrolase. (7/30)
The predicted amino acid sequence of the product of the acetate-inducible acu-8 gene of Neurospora crassa, previously of unknown function, has close homology to the recently published sequence of Saccharomyces cerevisiae acetyl-CoA hydrolase. An acu-8 mutant strain, previously characterized as acetate non-utilizing, shows strong growth-inhibition by acetate, but will use it as carbon source at low concentrations. The mutant was shown to be deficient in acetyl-CoA hydrolase and to accumulate acetyl-CoA when supplied with acetate. As in Saccharomyces, the Neurospora enzyme is acetate-inducible. (+info)Brassica juncea 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase 1: expression and characterization of recombinant wild-type and mutant enzymes. (8/30)
3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGS; EC 2.3.3.10) is the second enzyme in the cytoplasmic mevalonate pathway of isoprenoid biosynthesis, and catalyses the condensation of acetyl-CoA with acetoacetyl-CoA (AcAc-CoA) to yield S-HMG-CoA. In this study, we have first characterized in detail a plant HMGS, Brassica juncea HMGS1 (BjHMGS1), as a His6-tagged protein from Escherichia coli. Native gel electrophoresis analysis showed that the enzyme behaves as a homodimer with a calculated mass of 105.8 kDa. It is activated by 5 mM dithioerythreitol and is inhibited by F-244 which is specific for HMGS enzymes. It has a pH optimum of 8.5 and a temperature optimum of 35 degrees C, with an energy of activation of 62.5 J x mol(-1). Unlike cytosolic HMGS from chicken and cockroach, cations like Mg2+, Mn2+, Zn2+ and Co2+ did not stimulate His6-BjHMGS1 activity in vitro; instead all except Mg2+ were inhibitory. His6-BjHMGS1 has an apparent K(m-acetyl-CoA) of 43 microM and a V(max) of 0.47 micromol x mg(-1) x min(-1), and was inhibited by one of the substrates (AcAc-CoA) and by both products (HMG-CoA and HS-CoA). Site-directed mutagenesis of conserved amino acid residues in BjHMGS1 revealed that substitutions R157A, H188N and C212S resulted in a decreased V(max), indicating some involvement of these residues in catalytic capacity. Unlike His6-BjHMGS1 and its soluble purified mutant derivatives, the H188N mutant did not display substrate inhibition by AcAc-CoA. Substitution S359A resulted in a 10-fold increased specific activity. Based on these kinetic analyses, we generated a novel double mutation H188N/S359A, which resulted in a 10-fold increased specific activity, but still lacking inhibition by AcAc-CoA, strongly suggesting that His-188 is involved in conferring substrate inhibition on His6-BjHMGS1. Substitution of an aminoacyl residue resulting in loss of substrate inhibition has never been previously reported for any HMGS. (+info)Suematsu N, Isohashi F (2007). "Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase". Acta ... 2001). "Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase". Eur. J. Biochem. 268 (9): ... rat liver cytosolic acetyl-coenzyme A hydrolase". J. Chromatogr. B. 790 (1-2): 239-44. doi:10.1016/s1570-0232(03)00167-3. PMID ... "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029-32. doi:10.1194/jlr.E500003- ...
Acetyl-CoA hydrolase, palmitoyl-CoA hydrolase, succinyl-CoA hydrolase, formyl-CoA hydrolase, acyl-CoA hydrolase are a few ... Esterases, in turn, are one type of the several hydrolases known. Thioesterases exhibit Esterase activity (splitting of an ... Thioesterases or thiolester hydrolases are identified as members of E.C.3.1.2. ... "Evolutionary divergence and functions of the human acyl-CoA thioesterase gene ( ACOT ) family". Human Genomics. 4 (6): 411-20. ...
... thiolester hydrolases MeSH D08.811.277.352.897.075 --- acetyl-CoA hydrolase MeSH D08.811.277.352.897.700 --- palmitoyl-coa ... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 --- acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 --- acyl-coa ... acetyl-CoA C-acetyltransferase MeSH D08.811.913.050.134.105 --- amino-acid n-acetyltransferase MeSH D08.811.913.050.134.150 ... N-acetyl-beta-glucosaminyl)asparagine amidase MeSH D08.811.277.087.760 --- pyroglutamate hydrolase MeSH D08.811.277.087.831 ...
... acetyl-CoA hydrolase EC 3.1.2.2: palmitoyl-CoA hydrolase EC 3.1.2.3: succinyl-CoA hydrolase EC 3.1.2.4: 3-hydroxyisobutyryl-CoA ... bile-acid-CoA hydrolase EC 3.1.2.27: choloyl-CoA hydrolase EC 3.1.2.28: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase EC 3.1.2.29: ... formyl-CoA hydrolase EC 3.1.2.11: acetoacetyl-CoA hydrolase EC 3.1.2.12: S-formylglutathione hydrolase EC 3.1.2.13: S- ... ADP-dependent short-chain-acyl-CoA hydrolase EC 3.1.2.19: ADP-dependent medium-chain-acyl-CoA hydrolase EC 3.1.2.20: acyl-CoA ...
... acetyl-CoA acylase, acetyl coenzyme A hydrolase, acetyl coenzyme A deacylase, acetyl coenzyme A acylase, and acetyl-CoA thiol ... In enzymology, an acetyl-CoA hydrolase (EC 3.1.2.1) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O ⇌ {\ ... The systematic name of this enzyme class is acetyl-CoA hydrolase. Other names in common use include acetyl-CoA deacylase, ... the two substrates of this enzyme are acetyl-CoA and H2O, whereas its two products are CoA and acetate. It is present in many ...
This enzyme participates in citrate cycle (tca cycle). Gergely J, Hele P, Ramakrishnan CV (1952). "Succinyl and acetyl coenzyme ... In enzymology, a succinyl-CoA hydrolase (EC 3.1.2.3) is an enzyme that catalyzes the chemical reaction succinyl-CoA + H2O ⇌ {\ ... The systematic name of this enzyme class is succinyl-CoA hydrolase. Other names in common use include succinyl-CoA acylase, ... whereas its two products are CoA and succinate. This enzyme belongs to the family of hydrolases, specifically those acting on ...
... whereas its two products are acetyl-CoA carboxylase and phosphate. This enzyme belongs to the family of hydrolases, ... acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) is an enzyme that catalyzes the chemical reaction [acetyl-CoA carboxylase] ... acetyl-CoA carboxylase] + phosphate Thus, the two substrates of this enzyme are acetyl-CoA carboxylase phosphate and H2O, ... Krakower GR; Kim K-H (1980). "Purification and properties of acetyl-CoA carboxylase phosphatase". J. Biol. Chem. 256 (5): 2408- ...
I. Formyl coenzyme A, an intermediate in the formate-dependent decomposition of acetyl phosphate in Clostridium kluyveri". J. ... The systematic name of this enzyme class is formyl-CoA hydrolase. This enzyme is also called formyl coenzyme A hydrolase. This ... In enzymology, a formyl-CoA hydrolase (EC 3.1.2.10) is an enzyme that catalyzes the chemical reaction formyl-CoA + H2O ⇌ {\ ... whereas its two products are CoA and formate. This enzyme belongs to the family of hydrolases, specifically those acting on ...
... (abbreviated NAcGlu) is biosynthesized from glutamic acid and acetyl-CoA by the enzyme N-acetylglutamate ... The reverse reaction, hydrolysis of the acetyl group, is catalyzed by a specific hydrolase. NAcGlu activates carbamoyl ... Glutamate Glutamic acid "N-Acetyl-DL-glutamic acid - Compound Summary". PubChem Compound. USA: National Center for ...
Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen". J. Biol. Chem. 261 ( ... whereas its two products are 1-alkyl-2-acetyl-sn-glycerol and phosphate. This enzyme belongs to the family of hydrolases, ... Other names in common use include 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase, and alkylacetylglycerophosphate ... 1-alkyl-2-acetyl-sn-glycerol + phosphate Thus, the two substrates of this enzyme are 1-alkyl-2-acetyl-sn-glycero-3-phosphate ...
The enzyme is inhibited by high ratios of ATP:ADP, acetyl-CoA:CoA, and NADH:NAD, as high concentrations of ATP, acetyl-CoA, and ... These experiments have revealed that this single site alternates between two forms, which participate in ligase and hydrolase ... acetyl-CoA + oxaloacetate + H2O → citrate + CoA-SH acetyl-CoA Oxaloacetic acid Citric acid Oxaloacetate is regenerated after ... This induces the enzyme to change its conformation, and creates a binding site for the acetyl-CoA. Only when this citroyl-CoA ...
Acetoacetate is a ketone body, which is activated with succinyl-CoA, and thereafter it can be converted into acetyl-CoA, which ... Fumarylacetoacetate is finally split by the enzyme fumarylacetoacetate hydrolase through the addition of a water molecule. ...
... acetyl-CoA), which releases some energy. Finally, the acetyl group on the CoA is oxidised to water and carbon dioxide in the ... These digestive enzymes include proteases that digest proteins into amino acids, as well as glycoside hydrolases that digest ... and this breakdown process involves the release of significant amounts of acetyl-CoA, propionyl-CoA, and pyruvate, which can ... The glycerol enters glycolysis and the fatty acids are broken down by beta oxidation to release acetyl-CoA, which then is fed ...
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... Acyl-CoA thioesterase 9 is a protein that is encoded by the human ACOT9 gene. It is a member of the acyl-CoA thioesterase ...
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... as opposed to long-chain acyl-CoA synthetases, which ligate fatty acids to CoA, to produce the CoA ester. The role of the ACOT ... These enzymes have also been referred to in the literature as acyl-CoA hydrolases, ...
The cleavage of citryl-CoA to acetyl-CoA and oxaloacetate occurs in a two step process. First, citryl-coA synthetase catalyzes ... pathways while typical PSPs need Mg2+ for activity and are considered to be part of the haloacid dehalogenase-like hydrolase ... Novel proteins such as citryl-CoA synthetase (CCS) and ciitryl-CoA (CLL)are utilized within the reductive TCA cycle (Reverse ... 2004). "A novel enzyme, citryl-CoA lyase, catalyzing the second step of the citrate cleavage reaction in Hydrogenobacter ...
... propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, pyruvate carboxylase, and 2 forms of acetyl-CoA carboxylase.) ... peptidyl hydrolase biotinidase (BTD), and the protein ligase holocarboxylase synthetase. When any of these regulatory factors ... excretion of 3-hydroxyisovaleric acid and biotin in urine activity of propionyl-CoA carboxylase in lymphocytes In the United ...
Three acetyl-CoAs are converted inoto HMG-CoA by the cytosolic isoforms of thiolase and 3-hydroxy-3-methylglutaryl-CoA synthase ... JH acid is attached by JH epoxide hydrolase, which converts the epoxide group to a diol. The order of cleavage depends on the ... It is converted into acetyl-CoA, ADP, CO2, and oxaloacetate by ATP-citrate lyase, together with ATP and CoASH as substrates. ... The HMG-CoA is then reduced by NADPH to mevalonate by HMG-CoA reductase, the rate controlling enzyme of cholesterol ...
... acyl-CoA thioester hydrolases, and palmitoyl-CoA hydrolases. The reaction carried out by these enzymes is as follows: CoA ester ... These functions include allosteric regulation of enzymes such as acetyl-CoA carboxylase, hexokinase IV, and the citrate ... It is most active on myristoyl-CoA but also shows high activity on palmitoyl-CoA, stearoyl-CoA, and arachidoyl-CoA. The protein ... CoA) esters, such as acyl-CoAs, bile CoAs, and CoA esters of prostaglandins, to the corresponding free acid and CoA. ACOT2 ...
The liberated choline is taken up again by the pre-synaptic neuron and ACh is synthesized by combining with acetyl-CoA through ... AChE is a hydrolase that hydrolyzes choline esters. It has a very high catalytic activity - each molecule of AChE degrades ...
ACAT1: acetyl-Coenzyme A acetyltransferase 1 (acetoacetyl Coenzyme A thiolase) ACRV1: encoding protein Acrosomal protein SP-10 ... fatty acyl-coA reductase 1 FAT3: fat atypical cadherin 3 FHIP: FTS and Hook-interacting protein FNBP4: Formin-binding protein 4 ... encoding protein Ester hydrolase C11orf54 C11orf58: small acidic protein C11orf73: chromosome 11, open reading frame 73 ...
... is a hydrolase enzyme responsible for catalyzing the deacylation of N-acetyl-l-aspartate (N-acetylaspartate,NAA) into aspartate ... one hypothesis is that it is potentially used as a chemical reservoir that can be tapped into for acetate for acetyl-CoA ... Aspartoacylase prevents the build up of N-acetyl-L-aspartate in the brain. N-acetyl-L-aspartate is one of the most abundant ... The zinc cofactor is used to lower the pKa of a ligated water so that an attack on N-acetyl-L-aspartate may occur and to ...
In the conversion sequence of acetyl-CoA to glucose, CYP2E1 transforms acetone via hydroxyacetone (acetol) into propylene ... He J, Wang C, Zhu Y, Ai D (Dec 2015). "Soluble epoxide hydrolase: A potential target for metabolic diseases". Journal of ... EDP and EEQ metabolites are short-lived, being inactivated within seconds or minutes of formation by epoxide hydrolases, ... Fleming I (Oct 2014). "The pharmacology of the cytochrome P450 epoxygenase/soluble epoxide hydrolase axis in the vasculature ...
Fatty acid synthesis is an anabolic process that starts from the conversion of acetyl-CoA to malonyl-CoA by acetyl-CoA ... both of which can inhibit dioxygenases or prolyl hydrolases that mediate the degradation of HIF proteins. HIF-1 could be ... Malonyl CoA leads to fatty acid synthesis (FAS) and is involved in the elongation of fatty acids through Fatty acid synthase ( ...
... the enzyme serine acetyltransferase catalyzes the transfer of acetyl group from acetyl-CoA onto L-serine to yield O-acetyl-L- ... Orotate phosphoribosyl hydrolase (OMP pyrophosphorylase) condenses orotate with PRPP to form orotidine-5'-phosphate. OMP ... In the case of NADH, the molecule transfers a hydrogen, whereas acetyl CoA transfers an acetyl group, and ATP transfers a ... The following reaction step, catalyzed by the enzyme O-acetyl serine (thiol) lyase, replaces the acetyl group of O-acetyl-L- ...
3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, ... EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list). *EC6 Ligases (list) ... The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons ...
... acetyl-CoA acylase, acetyl coenzyme A hydrolase, acetyl coenzyme A deacylase, acetyl coenzyme A acylase, and acetyl-CoA thiol ... In enzymology, an acetyl-CoA hydrolase (EC 3.1.2.1) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O ⇌ {\ ... The systematic name of this enzyme class is acetyl-CoA hydrolase. Other names in common use include acetyl-CoA deacylase, ... the two substrates of this enzyme are acetyl-CoA and H2O, whereas its two products are CoA and acetate. It is present in many ...
"Expression of a yeast acetyl CoA hydrolase in the mitochondrion, Plant Molecular Biology" on DeepDyve, the largest online ... Expression of a yeast acetyl CoA hydrolase in the mitochondrion. Expression of a yeast acetyl CoA hydrolase in the ... specific role of acetyl CoA in the mitochondria we exploited a transgenic approach to introduce a yeast acetyl CoA hydrolase ( ... specific role of acetyl CoA in the mitochondria we exploited a transgenic approach to introduce a yeast acetyl CoA hydrolase ( ...
Lee, F. J., Lin, L. W., Smith, J. A. (1990). "A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces ... Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid ... Acetyl-CoA hydrolase MTISNLLKQRVRYAPYLKKVKEAHELIPLFKNGQYLGWSGFTGVGTPKAVPEALIDHVEK ... Acetic acid + hydron + Coenzyme A ↔ Acetyl-CoA + water Acetyl-CoA + water → Acetic acid + hydron + Coenzyme A ...
... revealing that the disappearance of acetyl CH3 from acetyl Coenzyme A occurred concomitantly with the appearance of a CH3 peak ... This folate-dependent activity is exclusive to these two isoforms; no acetyl Coenzyme A hydrolysis was found when murine ... These data, together with the characterisation of a naphthoquinone inhibitor of folate-dependent acetyl Coenzyme A hydrolysis ... and facilitate acetyl Coenzyme A hydrolysis. The evidence presented in this paper adds to our growing understanding of the ...
Glucose-regulated promoter of yeast acetyl-CoA hydrolase. US5500361 *. Nov 12, 1992. Mar 19, 1996. E. I. Du Pont De Nemours And ... Procaryotic carbonyl hydrolases. US5316925 *. Dec 3, 1992. May 31, 1994. Davis Mark M. T-cell receptor specific for antigen ...
ANAD2_1_PE1014 SubName: Full=Acetyl-CoA hydrolase/transferase; (ANAD2_1.PE1014). Keywords: acetyl-CoA hydrolase/transferase; ... Hydrolase; Lipid A biosynthesis; Lipid synthesis. Organism: ANAEROMYXOBACTER DEHALOGENANS 2CP-1 8. ANAD2_1_PE1004 SubName: Full ... Hydrolase; Nucleotide-binding; SOS response. Organism: ANAEROMYXOBACTER DEHALOGENANS 2CP-1 6. ANAD2_1_PE1002 SubName: Full= ... Hydrolase; Nucleotide-binding; Keywords: SOS response. Organism: ANAEROMYXOBACTER DEHALOGENANS 2CP-1 5. ANAD2_1_PE1001 RecName ...
acetyl-CoA hydrolase. References in periodicals archive ? Reversible immobilization of glutaryl acylase on sepabeads coated ...
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A ( ... acetyl-CoA hydrolase activity Source: HGNC ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the ... acyl-CoA hydrolase activity Source: MGI ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, ... acyl-CoA metabolic process Source: HGNC ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function, ...
Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis.. Khandokar YB, Londhe A, ...
2-aminobenzoyl)acetyl-CoA hydrolase. Reaction(IUBMB). (2-aminobenzoyl)acetyl-CoA + H2O = (2-aminobenzoyl)acetate + CoA [RN: ... Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response ...
... acetyl-CoA hydrolase. Reaction: acetyl-CoA + H2O = CoA + acetate. Other name(s): acetyl-CoA deacylase; acetyl-CoA acylase; ... EC 3.1.2.1 acetyl-CoA hydrolase. EC 3.1.2.2 palmitoyl-CoA hydrolase. EC 3.1.2.3 succinyl-CoA hydrolase. EC 3.1.2.4 3- ... acetyl coenzyme A deacylase; acetyl coenzyme A acylase; acetyl-CoA thiol esterase. Systematic name: acetyl-CoA hydrolase. Links ... palmitoyl-CoA hydrolase. Reaction: palmitoyl-CoA + H2O = CoA + palmitate. Other name(s): long-chain fatty-acyl-CoA hydrolase; ...
ABAYE0257 putative acetyl-CoA hydrolase/transferase ABAYE3797 lldD; L-lactate dehydrogenase, FMN linked ABAYE3796 dld; D- ... K01895 ACSS; acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA ... acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA synthetase [EC:6.2.1.1] K01895 ACSS; acetyl-CoA synthetase [EC:6.2. ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00632 fadA; acetyl- ...
Cytoplasmic acetyl-CoA hydrolase 1. *cytosolic acetyl-CoA hydrolase. *hCACH-1. *StARD15 ...
Acetate generation in rat liver mitochondria: acetyl-CoA hydrolase activity is demonstrated by 3-ketoacyl-CoA thiolase. ... acetyl-CoA + H2O = CoA + acetate. the bifunctional enzyme is identical with a 3-ketoacyl-CoA thiolase isozyme, i.e. THL, EC 2.3 ...
GO:0003986 [acetyl-CoA hydrolase activity]. GO:0005102 [receptor binding]. GO:0005515 [protein binding]. GO:0005737 [cytoplasm] ... CoA hydrolase activity]. GO:0016290 [palmitoyl-CoA hydrolase activity]. GO:0016559 [peroxisome fission]. GO:0016787 [hydrolase ... acyl-CoA hydrolase activity]. GO:0052689 [carboxylic ester hydrolase activity]. GO:0052815 [medium-chain acyl-CoA hydrolase ... GO:0033540 [fatty acid beta-oxidation using acyl-CoA oxidase]. GO:0033882 [choloyl-CoA hydrolase activity]. GO:0035338 [long- ...
... hydrolases, placed in numerical order as determined by the ... EC 3.1.2.1: acetyl-CoA hydrolase * EC 3.1.2.2: palmitoyl-CoA ... EC 3.1.5: Triphosphoric Monoester Hydrolases. * EC 3.1.5.1: dGTPase EC 3.1.6: Sulfuric Ester Hydrolases. * EC 3.1.6.1: ... EC1 Oxidoreductases/list - EC2 Transferases/list - EC3 Hydrolases/list - EC4 Lyases/list - EC5 Isomerases/list - EC6 Ligases/ ... This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the ...
... acetyl-CoA hydrolase; MGG_05869 = importin domain-containing; MGG_01439 = inorganic phosphate transporter; MGG_04470 = ...
... acetyl-CoA acetyltransferase, acyl coenzyme A thioester hydrolase, and prolyl isomerase; spots 14 and 15, malate dehydrogenase ... and the neuron-specific ubiquitin C-terminal hydrolase 1 (PGP9.5, spot 20; Fig. 1B). Of note, as our analysis was performed ...
Suematsu N, Isohashi F (2007). "Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase". Acta ... 2001). "Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase". Eur. J. Biochem. 268 (9): ... rat liver cytosolic acetyl-coenzyme A hydrolase". J. Chromatogr. B. 790 (1-2): 239-44. doi:10.1016/s1570-0232(03)00167-3. PMID ... "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases". J Lipid Res. 46 (9): 2029-32. doi:10.1194/jlr.E500003- ...
Expression of a yeast acetyl CoA hydrolase in the mitochondrion of tobacco plants inhibits growth and restricts photosynthesis ... Almost all metabolites can be degraded to Acetyl-CoA, and Acetyl-CoA itself is the building block of many biochemical ... Russell, MJ; Martin, W. The rocky roots of the acetyl-CoA pathway. Trends Biochem. Sci 2004, 29, 358-363. [Google Scholar] ... Further candidate high energy compounds are thioesters such as Acetyl-CoA which is a central molecule of present metabolism [ ...
Acyl-CoA Thioesterase 9, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human ... GO annotations related to this gene include carboxylic ester hydrolase activity and acetyl-CoA hydrolase activity. ... A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases. (PMID: 16103133) Hunt MC … Alexson SE (Journal of lipid ... acetyl-CoA hydrolase activity. ISS. --. GO:0016787. hydrolase activity. IEA. --. GO:0047617. acyl-CoA hydrolase activity. TAS. ...
Leucine and Lysine Are Degraded to Acetoacetate and/or Acetyl-CoA. Tryptophan Is Degraded to Alanine and Acetyl-CoA. ... metabolite is synthesized from glutamate and acetylCoA by N-acetylglutamate synthase and hydroliyzed by a specific hydrolase. ... is broken down to succinyl-CoA and acetyl-CoA and hence is a precursor of both carbohydrates and ketone bodies. The remaining ... 3.7 Tryptophan Is Degraded to Alanine and Acetyl-CoA. *3.8 Phenylalanine and Tyrosine Are Degraded to Fumarate and Acetoacetate ...
2015 NatB domain-containing CRA-1 antagonizes hydrolase ACER-1 linking acetyl-CoA metabolism to the initiation of recombination ...
oho:Oweho_3154 acetyl-CoA hydrolase 423 103 ( -) 29 0.579 38 -, 1 smon:AWR27_23735 hypothetical protein 158 103 ( -) 29 0.408 ... cdiv:CPM_1104 acyl-CoA synthetase (AMP-forming)/AMP-aci K01897 566 123 ( -) 34 0.315 73 -, 1 ble:BleG1_2449 hypothetical ... ddh:Desde_1771 acyl-CoA synthetase (AMP-forming)/AMP-ac K01897 548 112 ( -) 31 0.303 66 -, 1 seon:BWZ22_14460 mechanosensitive ...
... acetyl-CoA hydrolase (EZQ12320; spot 15) that catalyzes the chemical reaction: acetyl-CoA + H2O = CoA + acetate; (ii) the fatty ... catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. Beta-oxidation is the process where fatty acid ... molecules are broken down to generate acetyl-CoA as well as NADH, FADH2, which then enter the citric acid cycle and the ...
TransferasePyruvateLinking acetyl-CoA metabolismHydrolysisCarboxylic ester hydrolase activityCarboxylaseDehydrogenaseLigaseEnzymesMitochondrialAcylaseThiolaseMitochondriaSynthesisPropionyl-CoAGlutathioneEncodesHydroxybutyrate-dimer hydDeficiencyBiosynthesisLong-chainProteinDegradationEpoxide hydrolaseSaccharomycesFatty acylSystematicIntracellularMolecularSubstrateBelongsEstersLiver
- The de novo pathway utilizes 1-alkyl-2-acetyl- sn -glycerol and CDP-choline as substrates of a DTT-insensitive phosphocholine transferase (PAF-PCT). (springer.com)
- KEGG (Kyoto Encyclopedia of Genes and Genomes) analysis showed that 1-acyl-sn-glycerol-3-phosphate acyltransferase ( LPAAT ), phospholipase D, acetyl-CoA carboxylase carboxyltransferase beta subunit, 3-hydroxyisobutyryl-CoA hydrolase-like and pyruvate dehydrogenase E1 β subunit were associated with fatty acid biosynthesis or metabolism. (biomedcentral.com)
- This step is the final one in the glycolytic pathway, which produces pyruvate molecules that can be converted, as acetyl CoA , to ATP. (wikidoc.org)
- NatB domain-containing CRA-1 antagonizes hydrolase ACER-1 linking acetyl-CoA metabolism to the initiation of recombination during C. elegans meiosis. (bio-protocol.org)
- Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. (uniprot.org)
- The acyl-CoA thioesterase gene ( ACOT ) family encodes enzymes that catalyse the hydrolysis of acyl-CoA thioester compounds, also known as activated fatty acids, to their corresponding non-esterified (free) fatty acid and coenzyme A (CoASH). (biomedcentral.com)
- Only when this citroyl-CoA has formed will another conformational change cause thioester hydrolysis and release coenzyme A. This ensures that the energy released from the thioester bond cleavage will drive the condensation. (wikipedia.org)
- This gene encodes the enzyme responsible for hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. (mybiosource.com)
- GO annotations related to this gene include carboxylic ester hydrolase activity and acetyl-CoA hydrolase activity . (genecards.org)
- 47, Last updated, Version 1) DE Yeast DNA for acetyl CoA carboxylase, partial cds. (bio.net)
- Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. (mybiosource.com)
- Enzymes for further transformation were detected in cell extract, i.e., 4-fluorocinnamoyl-CoA hydratase, 4-fluorophenyl-β-hydroxy propionyl-CoA dehydrogenase, and 4-fluorophenyl-β-keto propionyl-CoA thiolase. (asm.org)
- Degradation of 4-fluorocinnamic acid by strain G1 occurred through a β-oxidation mechanism and started with the formation of 4-fluorocinnamoyl-coenzyme A (CoA), as indicated by the presence of 4-fluorocinnamoyl-CoA ligase. (asm.org)
- Many of them were enzymes in primary metabolism and other processes that affect the intracellular level of acetyl-CoA or NADPH. (biomedcentral.com)
- Acyl-CoA thioesterases (ACOTs) represent a group of enzymes that metabolise acyl-CoA esters to their corresponding non-esterified fatty acid and coenzyme A (CoASH). (biomedcentral.com)
- These enzymes are members of the α / β -hydrolase fold enzyme superfamily, which includes other esterase-activity-exhibiting enzymes such as carboxylesterases and lipases. (biomedcentral.com)
- 2.3.1.5) [ 1 ] are drug metabolising enzymes which catalyse the conjugation of an acetyl group from acetyl Coenzyme A (AcCoA) to arylamines, hydrazines and N- hydroxyarylamines. (biomedcentral.com)
- The enzyme is a hydrolase under the international classification of enzymes. (wikidoc.org)
- Both enzymes have been characterized as 2-hydroxy-6-oxohepta-2,4-dienoate hydrolases with low activity toward 2-hydroxy-6-oxophenylhexa-2,4-dienoate (the substrate of BphD), but EtbD2 and EtbD1 convert the latter compound with 11 and 3.3% relative activity, respectively (Yamada et al. (alpfmedical.info)
- The protein encoded by this gene is a mitochondrial acyl-CoA thioesterase of unknown function. (genecards.org)
- MBS7246273 is a ready-to-use microwell, strip plate Competitive ELISA (enzyme-linked immunosorbent assay) Kit for analyzing the presence of the 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (HIBCH) ELISA Kit target analytes in biological samples. (mybiosource.com)
- Other names in common use include acetyl-CoA deacylase, acetyl-CoA acylase, acetyl coenzyme A hydrolase, acetyl coenzyme A deacylase, acetyl coenzyme A acylase, and acetyl-CoA thiol esterase. (wikipedia.org)
- the bifunctional enzyme is identical with a 3-ketoacyl-CoA thiolase isozyme, i.e. (brenda-enzymes.org)
- fernie, Alisdair 2004-12-30 00:00:00 Acetyl Coenzyme A (acetyl CoA) is required in the mitochondria to fuel the operation of the Krebs cycle and within the cytosolic, peroxisomal and plastidial compartments wherein it acts as the immediate precursor for a wide range of anabolic functions. (deepdyve.com)
- To determine the specific role of acetyl CoA in the mitochondria we exploited a transgenic approach to introduce a yeast acetyl CoA hydrolase (EC 3.1.2.1. (deepdyve.com)
- 2. Berge, R.K. and Farstad, M. Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria. (qmul.ac.uk)
- Cytosolic acetyl-coenzyme A (Ac-CoA), a central precursor for lipid synthesis, is primarily made from mitochondria-derived citrate by ATP-citrate lyase (ACL) in cells with sufficient nutrients. (grantome.com)
- Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. (ymdb.ca)
- Background: Fatty acid synthase (FASN) catalyzes the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA. (cellsignal.com)
- Carman AJ, Vylkova S, Lorenz MC: Role of acetyl coenzyme A synthesis and breakdown in alternative carbon source utilization in Candida albicans. (gp120-inhibitors.com)
- Propionyl-CoA, also known as propionyl-coa, belongs to the class of organic compounds known as acyl coas. (bovinedb.ca)
- Propionyl-CoA is possibly soluble (in water) and a strong basic compound (based on its pKa). (bovinedb.ca)
- Propionyl-CoA participates in a number of enzymatic reactions, within cattle. (bovinedb.ca)
- In cattle, propionyl-CoA is involved in the metabolic pathway called the oxidation OF branched-chain fatty acids pathway. (bovinedb.ca)
- Propionyl-CoA is a potentially toxic compound. (bovinedb.ca)
- Substrates of 15 of these 27 groupings contain coenzyme A (CoA), two contain acyl carrier proteins (ACPs), four have glutathione or its derivatives, one has ubiquitin, and two contain other moieties. (axonmedchem.com)
- These reactions utilize energy from "activated" forms of the endogenous compounds (ie, acetyl-CoA, UDP-glucuronate, glutathione). (mhmedical.com)
- A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces cerevisiae. (ymdb.ca)
- The body metabolizes butyrate and produce D-β-hydroxybutyrate through the aid of the enzyme, hydroxybutyrate-dimer hydrolase . (biology-online.org)
- Mutations in this gene have been associated with 3-hyroxyisobutyryl-CoA hydrolase deficiency. (mybiosource.com)
- Also known as Alpha/beta hydrolase psoB (Pseurotin biosynthesis protein B). (mybiosource.com)
- Also hydrolyses CoA thioesters of other long-chain fatty acids. (qmul.ac.uk)
- Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. (genome.jp)
- ACOT9 (Acyl-CoA Thioesterase 9) is a Protein Coding gene. (genecards.org)
- This part contains the promoter BBa_J23119 , RBS* BBa_K2924009 , the coding region of Acyl-[acyl-carrier-protein] hydrolase from Cuphea hookeriana BBa_K2924001 and the double terminator BBa_B0015 . (igem.org)
- They hydrolyze acetyl-CoA esters or acyl carrier protein esters to the corresponding free fatty acid and the Coenzyme A or the acyl carrier protein. (igem.org)
- 47, Last updated, Version 1) DE Yeast DNA for TPR protein, YER049W, homology to ubiquitin DE carboxyl-terminal hydrolase. (bio.net)
- The acetyl-CoA degradation and related genes are shown in more detail (boxed). (nih.gov)
- Secondary control of the JH titre found in the haemolymph of the developing insect is metabolic inactivation of JH by JH-specific esterase and juvenile hormone epoxide hydrolase. (wikipedia.org)
- Fleck CB, Brock M: Re-characterisation Sapanisertib solubility dmso of Saccharomyces cerevisiae Ach1p: Fungal CoA-transferases are involved in acetic acid detoxification. (gp120-inhibitors.com)
- Buu LM, Chen YC, Lee FJS: Functional characterization and localization of acetyl-CoA hydrolase, Ach1p, in Saccharomyces cerevisiae. (gp120-inhibitors.com)
- ACOT activity helps to regulate cellular pools, as well as proper ratios, of activated fatty acyl-CoAs (acyl-CoA esters), free fatty acids (non-esterified fatty acids) and CoASH. (biomedcentral.com)
- The systematic name of this enzyme class is acetyl-CoA hydrolase. (wikipedia.org)
- Changes in the balance of intracellular metabolites towards a higher level of carbon passing through acetyl-CoA and a high capacity to regenerate NADPH during growth on medium with starch and lactate were found to be the likely cause of this effect. (biomedcentral.com)
- This list contains a list of EC numbers for the third group, EC 3 , hydrolases , placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. (bionity.com)
- Clinicians will find this book useful for understanding molecular aspects of neurodegeneration in acute neural trauma and neurodegenerative diseases that are mediated by plamalogen-selective phospholipases A 2 and PAF acetyl hydrolases. (wisepress.com)
- Remarkably, FlK does not accept acetyl-coenzyme A as a substrate. (rcsb.org)
- This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. (wikipedia.org)
- Belongs to the glycosyl hydrolase 84 family. (abcam.com)
- 3. Miyazawa, S., Furuta, S. and Hashimoto, T. Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators. (qmul.ac.uk)