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.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.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.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.Coenzyme APhosphatidylcholine-Sterol O-Acyltransferase: An enzyme secreted from the liver into the plasma of many mammalian species. It catalyzes the esterification of the hydroxyl group of lipoprotein cholesterol by the transfer of a fatty acid from the C-2 position of lecithin. In familial lecithin:cholesterol acyltransferase deficiency disease, the absence of the enzyme results in an excess of unesterified cholesterol in plasma. EC 2.3.1.43.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.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.Lecithin Acyltransferase Deficiency: An autosomal recessively inherited disorder caused by mutation of LECITHIN CHOLESTEROL ACYLTRANSFERASE that facilitates the esterification of lipoprotein cholesterol and subsequent removal from peripheral tissues to the liver. This defect results in low HDL-cholesterol level in blood and accumulation of free cholesterol in tissue leading to a triad of CORNEAL OPACITY, hemolytic anemia (ANEMIA, HEMOLYTIC), and PROTEINURIA.1-Acylglycerophosphocholine O-Acyltransferase: An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.Pyruvate 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.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.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.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.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.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.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)Malonyl Coenzyme A: A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.1-Acylglycerol-3-Phosphate O-Acyltransferase: An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. This enzyme has alpha, beta, gamma, delta and epsilon subunits.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.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.Acetyltransferases: Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.Magnesium Compounds: Inorganic compounds that contain magnesium as an integral part of the molecule.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.Acylation: The addition of an organic acid radical into a molecule.Kinetics: The rate dynamics in chemical or physical systems.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.Lipid Metabolism: Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.Fatty Acid Synthases: Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.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.Rhizobium etli: A species of gram-negative bacteria and nitrogen innoculant of PHASEOLUS VULGARIS.Cholesterol: The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.Palmitoyl Coenzyme A: A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.Mevalonic AcidGlycerophosphates: Any salt or ester of glycerophosphoric acid.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.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)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)Apolipoprotein A-I: The most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. This protein serves as an acceptor for CHOLESTEROL released from cells thus promoting efflux of cholesterol to HDL then to the LIVER for excretion from the body (reverse cholesterol transport). It also acts as a cofactor for LECITHIN CHOLESTEROL ACYLTRANSFERASE that forms CHOLESTEROL ESTERS on the HDL particles. Mutations of this gene APOA1 cause HDL deficiency, such as in FAMILIAL ALPHA LIPOPROTEIN DEFICIENCY DISEASE and in some patients with TANGIER DISEASE.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Carbon 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.TriglyceridesMitochondria, 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)CitratesRetinol 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.Acetylation: Formation of an acetyl derivative. (Stedman, 25th ed)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.Acetylesterase: An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.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.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.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.EstersCarbon 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.Carnitine Acyltransferases: Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.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.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.Penicillium chrysogenum: A mitosporic fungal species used in the production of penicillin.Hydroxymethylglutaryl CoA Reductases: Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.Organosilicon Compounds: Organic compounds that contain silicon as an integral part of the molecule.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.Lipoproteins, HDL: A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. HDL lipoproteins, synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). Their major protein component is APOLIPOPROTEIN A-I. HDL also shuttle APOLIPOPROTEINS C and APOLIPOPROTEINS E to and from triglyceride-rich lipoproteins during their catabolism. HDL plasma level has been inversely correlated with the risk of cardiovascular diseases.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.Dihydroxyacetone Phosphate: An important intermediate in lipid biosynthesis and in glycolysis.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.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.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.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.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Lysophosphatidylcholines: Derivatives of PHOSPHATIDYLCHOLINES obtained by their partial hydrolysis which removes one of the fatty acid moieties.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)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.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).Lipoproteins: Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes.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.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.Hypolipoproteinemias: Conditions with abnormally low levels of LIPOPROTEINS in the blood. This may involve any of the lipoprotein subclasses, including ALPHA-LIPOPROTEINS (high-density lipoproteins); BETA-LIPOPROTEINS (low-density lipoproteins); and PREBETA-LIPOPROTEINS (very-low-density lipoproteins).Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.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.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.Lysophospholipase: An enzyme that catalyzes the hydrolysis of a single fatty acid ester bond in lysoglycerophosphatidates with the formation of glyceryl phosphatidates and a fatty acid. EC 3.1.1.5.Palmitic Acids: A group of 16-carbon fatty acids that contain no double bonds.Corneal Opacity: Disorder occurring in the central or peripheral area of the cornea. The usual degree of transparency becomes relatively opaque.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.Oleic Acids: A group of fatty acids that contain 18 carbon atoms and a double bond at the omega 9 carbon.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.Carnitine O-Acetyltransferase: An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.Apolipoproteins: Protein components on the surface of LIPOPROTEINS. They form a layer surrounding the hydrophobic lipid core. There are several classes of apolipoproteins with each playing a different role in lipid transport and LIPID METABOLISM. These proteins are synthesized mainly in the LIVER and the INTESTINES.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)Monoglycerides: GLYCEROL esterified with a single acyl (FATTY ACIDS) chain.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.Acyl Carrier Protein: Consists of a polypeptide chain and 4'-phosphopantetheine linked to a serine residue by a phosphodiester bond. Acyl groups are bound as thiol esters to the pantothenyl group. Acyl carrier protein is involved in every step of fatty acid synthesis by the cytoplasmic system.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.DiglyceridesApolipoproteins A: Structural proteins of the alpha-lipoproteins (HIGH DENSITY LIPOPROTEINS), including APOLIPOPROTEIN A-I and APOLIPOPROTEIN A-II. They can modulate the activity of LECITHIN CHOLESTEROL ACYLTRANSFERASE. These apolipoproteins are low in atherosclerotic patients. They are either absent or present in extremely low plasma concentration in TANGIER DISEASE.Dithionitrobenzoic Acid: A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.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).Lipoylation: Covalent attachment of LIPIDS and FATTY ACIDS to other compounds and PROTEINS.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)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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Microbodies: Electron-dense cytoplasmic particles bounded by a single membrane, such as PEROXISOMES; GLYOXYSOMES; and glycosomes.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)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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.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.Energy Metabolism: The chemical reactions involved in the production and utilization of various forms of energy in cells.Lipoproteins, LDL: A class of lipoproteins of small size (18-25 nm) and light (1.019-1.063 g/ml) particles with a core composed mainly of CHOLESTEROL ESTERS and smaller amounts of TRIGLYCERIDES. The surface monolayer consists mostly of PHOSPHOLIPIDS, a single copy of APOLIPOPROTEIN B-100, and free cholesterol molecules. The main LDL function is to transport cholesterol and cholesterol esters to extrahepatic tissues.Vitamin A: Retinol and derivatives of retinol that play an essential role in metabolic functioning of the retina, the growth of and differentiation of epithelial tissue, the growth of bone, reproduction, and the immune response. Dietary vitamin A is derived from a variety of CAROTENOIDS found in plants. It is enriched in the liver, egg yolks, and the fat component of dairy products.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.Lysophospholipids: Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal.Polyketide Synthases: Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Palmitates: Salts and esters of the 16-carbon saturated monocarboxylic acid--palmitic acid.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.Phosphatidic Acids: Fatty acid derivatives of glycerophosphates. They are composed of glycerol bound in ester linkage with 1 mole of phosphoric acid at the terminal 3-hydroxyl group and with 2 moles of fatty acids at the other two hydroxyl groups.Ethylmaleimide: A sulfhydryl reagent that is widely used in experimental biochemical studies.Sterol Esterase: An enzyme that catalyzes the hydrolysis of CHOLESTEROL ESTERS and some other sterol esters, to liberate cholesterol plus a fatty acid anion.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)Seeds: The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.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)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.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.Lipoprotein-X: An abnormal lipoprotein present in large amounts in patients with obstructive liver diseases such as INTRAHEPATIC CHOLESTASIS. LP-X derives from the reflux of BILE lipoproteins into the bloodstream. LP-X is a low-density lipoprotein rich in free CHOLESTEROL and PHOSPHOLIPIDS but poor in TRIGLYCERIDES; CHOLESTEROL ESTERS; and protein.Phosphatidate Phosphatase: A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyzes the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate. EC 3.1.3.4.Palmitic Acid: A common saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.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.Octoxynol: Nonionic surfactant mixtures varying in the number of repeating ethoxy (oxy-1,2-ethanediyl) groups. They are used as detergents, emulsifiers, wetting agents, defoaming agents, etc. Octoxynol-9, the compound with 9 repeating ethoxy groups, is a spermatocide.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.Glycerides: GLYCEROL esterified with FATTY ACIDS.Phospholipases: A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-.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.Lipid A: Lipid A is the biologically active component of lipopolysaccharides. It shows strong endotoxic activity and exhibits immunogenic properties.Penicillium: A mitosporic Trichocomaceae fungal genus that develops fruiting organs resembling a broom. When identified, teleomorphs include EUPENICILLIUM and TALAROMYCES. Several species (but especially PENICILLIUM CHRYSOGENUM) are sources of the antibiotic penicillin.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)Apolipoprotein A-II: The second most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. It has a high lipid affinity and is known to displace APOLIPOPROTEIN A-I from HDL particles and generates a stable HDL complex. ApoA-II can modulate the activation of LECITHIN CHOLESTEROL ACYLTRANSFERASE in the presence of APOLIPOPROTEIN A-I, thus affecting HDL metabolism.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.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Cholesterol, Dietary: Cholesterol present in food, especially in animal products.Pantetheine: An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.Cholesterol Ester Transfer Proteins: Proteins that bind to and transfer CHOLESTEROL ESTERS between LIPOPROTEINS such as LOW-DENSITY LIPOPROTEINS and HIGH-DENSITY LIPOPROTEINS.Thiolester HydrolasesArachis hypogaea: A plant species of the family FABACEAE that yields edible seeds, the familiar peanuts, which contain protein, oil and lectins.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.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Molecular Weight: The sum of the weight of all the atoms in a molecule.Cyclohexanes: Six-carbon alicyclic hydrocarbons.Carnitine O-Palmitoyltransferase: An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.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.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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Plasmalogens: GLYCEROPHOSPHOLIPIDS in which one of the two acyl chains is attached to glycerol with an ether alkenyl linkage instead of an ester as with the other glycerophospholipids.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Lipoproteins, VLDL: A class of lipoproteins of very light (0.93-1.006 g/ml) large size (30-80 nm) particles with a core composed mainly of TRIGLYCERIDES and a surface monolayer of PHOSPHOLIPIDS and CHOLESTEROL into which are imbedded the apolipoproteins B, E, and C. VLDL facilitates the transport of endogenously made triglycerides to extrahepatic tissues. As triglycerides and Apo C are removed, VLDL is converted to INTERMEDIATE-DENSITY LIPOPROTEINS, then to LOW-DENSITY LIPOPROTEINS from which cholesterol is delivered to the extrahepatic tissues.Hydroxycholesterols: Cholesterol which is substituted by a hydroxy group in any position.Deoxycholic Acid: A bile acid formed by bacterial action from cholate. It is usually conjugated with glycine or taurine. Deoxycholic acid acts as a detergent to solubilize fats for intestinal absorption, is reabsorbed itself, and is used as a choleretic and detergent.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.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Clofibrate: A fibric acid derivative used in the treatment of HYPERLIPOPROTEINEMIA TYPE III and severe HYPERTRIGLYCERIDEMIA. (From Martindale, The Extra Pharmacopoeia, 30th ed, p986)Mortierella: A genus of zygomycetous fungi of the family Mortierellaceae, order MUCORALES. Its species are abundant in soil and can cause rare infections in humans and animals. Mortierella alpinais is used for production of arachidonic acid.Bacterial Proteins: Proteins found in any species of bacterium.Fatty Alcohols: Usually high-molecular-weight, straight-chain primary alcohols, but can also range from as few as 4 carbons, derived from natural fats and oils, including lauryl, stearyl, oleyl, and linoleyl alcohols. They are used in pharmaceuticals, cosmetics, detergents, plastics, and lube oils and in textile manufacture. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Glycerol: A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.Chondrodysplasia Punctata, Rhizomelic: An autosomal recessive form of CHONDRODYSPLASIA PUNCTATA characterized by defective plasmalogen biosynthesis and impaired peroxisomes. Patients have shortened proximal limbs and severely disturbed endochondral bone formation. The metabolic defects associated with the impaired peroxisomes are present only in the rhizomelic form of chondrodysplasia punctata. (From Scriver et al, Metabolic Basis of Inherited Disease, 6th ed, p1497)Cell Line: Established cell cultures that have the potential to propagate indefinitely.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.Polyethylene Glycols: Polymers of ETHYLENE OXIDE and water, and their ethers. They vary in consistency from liquid to solid depending on the molecular weight indicated by a number following the name. They are used as SURFACTANTS, dispersing agents, solvents, ointment and suppository bases, vehicles, and tablet excipients. Some specific groups are NONOXYNOLS, OCTOXYNOLS, and POLOXAMERS.Lipid Metabolism, Inborn Errors: Errors in the metabolism of LIPIDS resulting from inborn genetic MUTATIONS that are heritable.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Retinol-Binding Proteins, Cellular: A subclass of retinol-binding proteins that take part in the intracellular storage and transport of RETINOL. They are both functionally and structurally distinct from PLASMA RETINOL-BINDING PROTEINS.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.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.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.Harderian Gland: A sebaceous gland that, in some animals, acts as an accessory to the lacrimal gland. The harderian gland excretes fluid that facilitates movement of the third eyelid.Cardiolipins: Acidic phospholipids composed of two molecules of phosphatidic acid covalently linked to a molecule of glycerol. They occur primarily in mitochondrial inner membranes and in bacterial plasma membranes. They are the main antigenic components of the Wassermann-type antigen that is used in nontreponemal SYPHILIS SERODIAGNOSIS.Diacylglycerol Cholinephosphotransferase: An enzyme that catalyzes the synthesis of phosphatidylcholines from CDPcholine and 1,2-diacylglycerols. EC 2.7.8.2.Cholesterol, HDL: Cholesterol which is contained in or bound to high-density lipoproteins (HDL), including CHOLESTEROL ESTERS and free cholesterol.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.Animal Population Groups: Animals grouped according to ecological, morphological or genetic populations.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Phospholipases A: Phospholipases that hydrolyze one of the acyl groups of phosphoglycerides or glycerophosphatidates.Receptors, LDL: Receptors on the plasma membrane of nonhepatic cells that specifically bind LDL. The receptors are localized in specialized regions called coated pits. Hypercholesteremia is caused by an allelic genetic defect of three types: 1, receptors do not bind to LDL; 2, there is reduced binding of LDL; and 3, there is normal binding but no internalization of LDL. In consequence, entry of cholesterol esters into the cell is impaired and the intracellular feedback by cholesterol on 3-hydroxy-3-methylglutaryl CoA reductase is lacking.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.Glycerylphosphorylcholine: A component of PHOSPHATIDYLCHOLINES or LECITHINS, in which the two hydroxy groups of GLYCEROL are esterified with fatty acids. (From Stedman, 26th ed) It counteracts the effects of urea on enzymes and other macromolecules.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.Carboxylic Ester Hydrolases: Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.Sulfonic Acids: Inorganic or organic oxy acids of sulfur which contain the RSO2(OH) radical.Anticholesteremic Agents: Substances used to lower plasma CHOLESTEROL levels.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Peroxisomes: Microbodies which occur in animal and plant cells and in certain fungi and protozoa. They contain peroxidase, catalase, and allied enzymes. (From Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed)TriosesIsoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Radioisotope Dilution Technique: Method for assessing flow through a system by injection of a known quantity of radionuclide into the system and monitoring its concentration over time at a specific point in the system. (From Dorland, 28th ed)Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Fatty Acids, Nonesterified: FATTY ACIDS found in the plasma that are complexed with SERUM ALBUMIN for transport. These fatty acids are not in glycerol ester form.Apolipoproteins B: Major structural proteins of triacylglycerol-rich LIPOPROTEINS. There are two forms, apolipoprotein B-100 and apolipoprotein B-48, both derived from a single gene. ApoB-100 expressed in the liver is found in low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). ApoB-48 expressed in the intestine is found in CHYLOMICRONS. They are important in the biosynthesis, transport, and metabolism of triacylglycerol-rich lipoproteins. Plasma Apo-B levels are high in atherosclerotic patients but non-detectable in ABETALIPOPROTEINEMIA.

Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver. (1/166)

The specific activities and substrate specificities of 3-oxoacyl-CoA thiolase A (thiolase A) purified from normal rat liver peroxisomes and 3-oxoacyl-CoA thiolase B (thiolase B) isolated from livers of rats treated with the peroxisome proliferator clofibrate were virtually identical. The enzymes could be distinguished by their N-terminal amino acid sequences, their isoelectric points and their stability, the latter being higher for thiolase A. Contrary to thiolase B, which showed a marked cold lability in the presence of KCl by dissociating into monomers with poor activity, thiolase A retained its full activity and its homodimeric structure under these conditions.  (+info)

Expression and intracellular processing of the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase in transfected mouse L-cell fibroblasts. (2/166)

Although the sterol carrier protein 2 (SCP-2) gene encodes for two proteins, almost nothing is known of the function and potential processing of the larger transcript corresponding to the 58 kDa sterol carrier protein-2/3-oxoacyl-CoA thiolase (SCP-x), in intact cells. L-cell fibroblasts transfected with cDNA encoding for the 58 kDa SCP-x protein had a 4.5-fold increase in SCP-x mRNA transcript levels. Western blot analysis showed SCP-x protein expression reached 0.011% of total protein, representing a 4.1-fold increase over basal levels. Surprisingly, the 13.2 kDa SCP-2 protein also increased 2-fold in the transfected cells. This was consistent with part of the 58 kDa SCP-x being proteolytically processed to 13.2 kDa SCP-2 as there was no evidence of an mRNA transcript corresponding to a 13.2/15.2 kDa gene product in the transfected L-cell clones. Confocal immunofluorescence microscopy of transfected L-cells showed that SCP-x/SCP-2 co-localized in highest concentration with catalase in peroxisomes, but significant amounts appeared extra-peroxisomal. Overexpression of SCP-x significantly altered cholesterol uptake and metabolism. Uptake of exogenous [3H]cholesterol and total cholesterol mass were increased 1.9- and 1.4-fold, respectively, in SCP-x expressors. Although cholesterol ester mass was unaltered, incorporation of exogenous [3H]cholesterol and [3H]oleic acid into cholesteryl esters increased 2.3- and 2.5-fold, respectively. These results from intact cells suggest the 13.2 kDa SCP-2 can arise from the larger SCP-2 gene product and indicate a role for the 58 kDa SCP-x protein in cholesterol uptake and intracellular cycling.  (+info)

Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. (3/166)

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)

Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain. (4/166)

The fibroblast growth factor (FGF) family is composed of polypeptides with sequence identity which signal through transmembrane tyrosine kinase receptors. We report here the purification from bovine brain microsomes of an FGF-2-binding complex composed of three proteins of apparent molecular masses 150 kDa, 79 kDa and 46 kDa. Only the 150 kDa and 79 kDa proteins bound FGF-2 in cross-linking and ligand-blotting experiments. Binding of FGF-2 to p79 is enhanced in the presence of calcium. Peptide sequences allowed the identification of p150 and the cloning of the cDNAs encoding p79 and p46. The deduced amino acid sequence of p79 reveals high similarity to those of gastrin-binding protein and mitochondrial enoyl-CoA hydratase/hydroxyacyl-CoA dehydrogenase. p46 is similar to mitochondrial ketoacyl-CoA thiolase. Stable transfection of FR3T3 rat fibroblast cells with p79 cDNA analysed by electron microscopy following immunolabelling of ultra-thin cryosections revealed a localization of p79 in the secretory pathway, mainly in the endoplasmic reticulum and the Golgi region, where it is specifically associated with the molecular chaperone calnexin. In vivo a protein similar to the Golgi protein MG-160 forms a complex with FGF-2 and p79.  (+info)

Type-II 3-oxoacyl-CoA thiolase of the nematode Caenorhabditis elegans is located in peroxisomes, highly expressed during larval stages and induced by clofibrate. (5/166)

We examined the expression and localization of type-II 3-oxoacyl-CoA thiolase in the nematode Caenorhabditis elegans. Type-II thiolase acts on 3-oxoacyl-CoA esters with a methyl group at the alpha carbon, whereas conventional thiolases do not. Mammalian type-II thiolase, which is also termed sterol carrier protein x (SCPx) or SCP2/3-oxoacyl-CoA thiolase, is located in the peroxisomes and involved in phytanic acid degradation and most probably in bile acid synthesis. The nematode enzyme lacks the SCP2 domain, which carries the peroxisomal-targeting signal, but produces bile acids in a cell-free system. Northern and Western blot analyses demonstrated that C. elegans expressed type-II thiolase throughout its life cycle, especially during the larval stages, and that the expression was significantly enhanced by the addition of clofibrate at 5 mM or more to the culture medium. Whole-mount in situ hybridization and immunostaining of L4 larvae revealed that the enzyme was mainly expressed in intestinal cells, which are multifunctional like many of the cell types in C. elegans. Subcellular fractionation and indirect immunoelectron microscopy of the nematode detected the enzyme in the matrix of peroxisomes. These results indicate the fundamental homology between mammalian SCPx and the nematode enzyme regardless of whether the SCP2 part is fused, suggesting their common physiological roles.  (+info)

Biochemical and genetic analyses of ferulic acid catabolism in Pseudomonas sp. Strain HR199. (6/166)

The gene loci fcs, encoding feruloyl coenzyme A (feruloyl-CoA) synthetase, ech, encoding enoyl-CoA hydratase/aldolase, and aat, encoding beta-ketothiolase, which are involved in the catabolism of ferulic acid and eugenol in Pseudomonas sp. strain HR199 (DSM7063), were localized on a DNA region covered by two EcoRI fragments (E230 and E94), which were recently cloned from a Pseudomonas sp. strain HR199 genomic library in the cosmid pVK100. The nucleotide sequences of parts of fragments E230 and E94 were determined, revealing the arrangement of the aforementioned genes. To confirm the function of the structural genes fcs and ech, they were cloned and expressed in Escherichia coli. Recombinant strains harboring both genes were able to transform ferulic acid to vanillin. The feruloyl-CoA synthetase and enoyl-CoA hydratase/aldolase activities of the fcs and ech gene products, respectively, were confirmed by photometric assays and by high-pressure liquid chromatography analysis. To prove the essential involvement of the fcs, ech, and aat genes in the catabolism of ferulic acid and eugenol in Pseudomonas sp. strain HR199, these genes were inactivated separately by the insertion of omega elements. The corresponding mutants Pseudomonas sp. strain HRfcsOmegaGm and Pseudomonas sp. strain HRechOmegaKm were not able to grow on ferulic acid or on eugenol, whereas the mutant Pseudomonas sp. strain HRaatOmegaKm exhibited a ferulic acid- and eugenol-positive phenotype like the wild type. In conclusion, the degradation pathway of eugenol via ferulic acid and the necessity of the activation of ferulic acid to the corresponding CoA ester was confirmed. The aat gene product was shown not to be involved in this catabolism, thus excluding a beta-oxidation analogous degradation pathway for ferulic acid. Moreover, the function of the ech gene product as an enoyl-CoA hydratase/aldolase suggests that ferulic acid degradation in Pseudomonas sp. strain HR199 proceeds via a similar pathway to that recently described for Pseudomonas fluorescens AN103.  (+info)

Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway. (7/166)

Organelle biogenesis and turnover are necessary to maintain biochemical processes that are appropriate to the needs of the eukaryotic cell. Specific degradation of organelles in response to changing environmental cues is one aspect of achieving proper metabolic function. For example, the yeast Saccharomyces cerevisiae adjusts the level of peroxisomes in response to differing nutritional sources. When cells are grown on oleic acid as the sole carbon source, peroxisome biogenesis is induced. Conversely, a subsequent shift to glucose-rich or nitrogen-limiting conditions results in peroxisome degradation. The degradation process, pexophagy, requires the activity of vacuolar hydrolases. In addition, peroxisome degradation is specific. Analyses of cellular marker proteins indicate that peroxisome degradation under these conditions occurs more rapidly and to a greater extent than mitochondrial, Golgi, or cytosolic protein delivery to the vacuole by the non-selective autophagy pathway. To elucidate the molecular mechanism of selective peroxisome degradation, we examined pexophagy in mutants that are defective in autophagy (apg) and the selective targeting of aminopeptidase I to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway. Inhibition of peroxisome degradation in cvt and apg mutants indicates that these pathways overlap and that peroxisomes are delivered to the vacuole by a mechanism that utilizes protein components of the Cvt/autophagy pathways.  (+info)

Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of beta oxidation of the intermediate benzylsuccinate. (8/166)

The pathway of anaerobic toluene oxidation to benzoyl coenzyme A (benzoyl-CoA) consists of an initial reaction catalyzed by benzylsuccinate synthase, a glycyl radical enzyme adding the methyl group of toluene to the double bond of a fumarate cosubstrate, and a subsequent beta-oxidation pathway of benzylsuccinate. Benzylsuccinate synthase has been studied in some detail, whereas the enzymes participating in beta oxidation of benzylsuccinate are unknown. We have investigated these enzymes by analyzing substrate-induced proteins in toluene-grown cells. Toluene-induced proteins were identified and N-terminally sequenced. Nine of these proteins are encoded by an 8.5-kb operon consisting of bbs (beta-oxidation of benzylsuccinate) genes whose products are apparently involved in the beta-oxidation pathway of benzylsuccinate. Two of the genes, bbsE and bbsF, code for the subunits of a succinyl-CoA:benzylsuccinate CoA-transferase whose activity was previously detected in toluene-grown Thauera aromatica. The bbsG gene codes for a specific benzylsuccinyl-CoA dehydrogenase, as confirmed by overexpression of the gene in Escherichia coli and detection of enzyme activity. The further enzymes of the pathway are probably encoded by bbsH (enoyl-CoA hydratase), bbsCD (3-hydroxyacyl-CoA dehydrogenase), and bbsB (3-oxoacyl-CoA thiolase). The operon contains two additional genes, bbsA and bbsI, for which no obvious function could be derived. The bbs operon is expressed only in toluene-grown cells and is regulated at the transcriptional level. Promoter mapping revealed a transcription start site upstream of the bbsA gene. This represents the first known promoter site in Thauera spp.  (+info)

... or 2M3HBA is a rare genetic condition. 2M3HBA results from a mutation (error) in a persons DNA. 2M3HBA is considered an organic acid condition because it leads to a buildup of harmful amounts of organic acids in the body. Protein in the food we eat is broken down into amino acids, or "building blocks". We typically eat more protein than needed; therefore we often have more amino acids than we need. Enzymes (special proteins) breakdown the extra amino acids into organic acids and ammonia, and then harmless products our body can get rid of. If one of the enzymes needed is missing or not working correctly, the amino acid is not broken all the way down and builds up in our system as organic acids. Although organic acids are only mild acids, both organic acids and ammonia can damage our bodies if too much builds up. In this case the enzyme, 2-methyl-3-hydroxybutyryl, is unable to break down the amino acid, isoleucine.. Signs of 2M3HBA typically begin to show during ...
A collection of disease information resources and questions answered by our Genetic and Rare Diseases Information Specialists for Beta ketothiolase deficiency
In the present report we describe a method for the complete purification of native sterol carrier protein 2/3-oxoacyl-CoA thiolase (SCP-2/thiolase) from normal rat liver peroxisomes. The isolation procedure is based on the alteration in chromatographic properties of the enzyme in the presence of low concentrations of CoA. The purified preparation of SCP-2/thiolase consisted of 58- and 46-kDa polypeptides. Peroxisomes prepared freshly from normal rat liver contained three SCP-2/thiolase isoforms, separable by conventional chromatography. Immunochemical, molecular sieving, and chemical cross-linking experiments indicated that these isoforms represent thiolytically active homo- and heterodimeric combinations of the 46- and 58-kDa subunits (2 x 58, 58-46, and 2 x 46-kDa proteins). (C) 2000 Academic Press ...
Shop Beta-ketothiolase ELISA Kit, Recombinant Protein and Beta-ketothiolase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
The ACAT1 gene is associated with autosomal recessive beta-ketothiolase deficiency (aka mitochondrial acetoacetyl-CoA thiolase deficiency) (MedGen UID: 280689).
The β-oxidation of valproic acid (VPA; 2-n-propylpentanoic acid) was investigated in vitro in intact rat liver mitochondria incubated with 3H-labelled VPA. The metabolism of [4,5-3H2]VPA and [2-3H]VPA was studied by analysing the different acyl-CoA intermediates formed by reverse-phase HPLC with radiochemical detection. Valproyl-CoA, Δ2(E)-valproyl-CoA,3-hydroxyvalproyl-CoA and 3-oxovalproyl-CoA (labelled and non-labelled) were determined using continuous on-line radiochemical and UV detection. The formation of these intermediates was investigated using the two tritiated precursors in respiratory states 3 and 4. Valproyl-CoA was present at highest concentrations under both conditions. Two distinct labelled peaks were found, which were identified as 3H2O and [4,5-3H2]3-oxo-VPA. The formation of 3H2O strongly suggested that VPA underwent complete β-oxidation and that [4,5-3H2]3-oxo-VPA was formed by hydrolysis of the corresponding thioester. The hypothesis that 3-oxovalproyl-CoA undergoes ...
Binds to the N-terminal PTS2-type peroxisomal targeting signal and plays an essential role in peroxisomal protein import essential for import of 3-oxoacyl-CoA thiolase (a PTS2-containing protein) into peroxisomes. May direct thiolase to peroxisomes by shuttling between the cytosol and peroxisomal membranes.
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. Involved in the aerobic and anaerobic degradation of long-chain fatty acids.
Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287 ...
3-ketothiolase deficiency (3KTD) [MIM:203750]: An inborn error of isoleucine catabolism characterized by intermittent ketoacidotic attacks associated with unconsciousness. Some patients die during an attack or are mentally retarded. Urinary excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine, butanone is increased. It seems likely that the severity of this disease correlates better with the environmental or acquired factors than with the ACAT1 genotype. {ECO:0000269,PubMed:1346617, ECO:0000269,PubMed:1715688, ECO:0000269,PubMed:7728148, ECO:0000269,PubMed:9744475}. Note=The disease is caused by mutations affecting the gene represented in this entry ...
Mitochondrial fatty-acid beta-oxidation (mFAO) plays a central role in mammalian energy metabolism. Multiple severe diseases are associated with defects in this pathway. Its kinetic structure is characterized by a complex wiring of which the functional implications have hardly been explored. Repetitive cycles of reversible reactions, each cycle shortening the fatty acid by two carbon atoms, evoke competition between intermediates of different chain lengths for a common set of promiscuous enzymes (enzymes with activity towards multiple substrates). In our validated kinetic model of the pathway, substrate overload causes a steep and detrimental flux decline. Here, we unravel the underlying mechanism and the role of enzyme promiscuity in it. Comparison of alternative model versions elucidated the role of promiscuity of individual enzymes. Promiscuity of the last enzyme of the pathway, medium-chain ketoacyl-CoA thiolase (MCKAT), was both necessary and sufficient to elicit the flux decline. ...
CP000859.PE558 Location/Qualifiers FT CDS_pept 625652..626875 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Dole_0558" FT /product="Thiolase" FT /note="PFAM: Thiolase; KEGG: bbr:BB1086 putative thiolase" FT /db_xref="EnsemblGenomes-Gn:Dole_0558" FT /db_xref="EnsemblGenomes-Tr:ABW66368" FT /db_xref="GOA:A8ZU56" FT /db_xref="InterPro:IPR002155" FT /db_xref="InterPro:IPR016039" FT /db_xref="InterPro:IPR020616" FT /db_xref="InterPro:IPR020617" FT /db_xref="UniProtKB/TrEMBL:A8ZU56" FT /protein_id="ABW66368.1" FT /translation="MRDVAIIGAGMTRFGKFPEKSIKDLVKESSQAAIKDAGIQPSDIQ FT AAYVGSAVAGLMTGQEMIKAQVTLSAMGIEAIPMYNVENACASSSSALNLAWTAVGAGI FT FDCVLVTGFEKLYDEDKKKSFAALGTAVDIELFKLFLAEFQKNQGKGESIIKEGSGQKR FT SVFMDMYAHYTKIYMDRYGLTQEHFARIAVKSHKNGALNPHSQYQEEVTLEQVLNSGDV FT SWPLTRMMCSPIGDGAAAVIVCSKEAAARFGARPVWIASSVVGSGKLSGDLEDTLTKRL FT APKAFEAAGIGPDDIDVIEVHDATSPSEIITLIELGLCPGADAPKWIDEGYMEIDGSRP FT SNTSGGLAAKGHPIGATGLGQVYEIVNQLRGTAGKRQVKNPKVGMTHNGGGILGVDAAA FT MALHVFKN" atgcgtgatg tggcaattat cggagcgggc ...
Looking for online definition of 3-ketoacyl-CoA thiolase in the Medical Dictionary? 3-ketoacyl-CoA thiolase explanation free. What is 3-ketoacyl-CoA thiolase? Meaning of 3-ketoacyl-CoA thiolase medical term. What does 3-ketoacyl-CoA thiolase mean?
Thiolase of Clostridium acetobutylicum is an important enzyme involved in both, acid and solvent fermentation. Two thiolase genes (thlA and thlB) have been cloned and sequenced from Clostridium acetobutylicum DSM 792, showing high homology to each other and to thiolases of PHA-synthesizing bacteria. The thlA gene is identical to the gene already cloned and sequenced from strain ATCC 824 (Stim- Herndon et al., 1995, Gene 154: 81-85). Using primer extension and S1 nuclease analysis a transcriptional start site was identified 102 bp upstream of the thlA start codon. This site was preceded by a region that exhibits high similarity to the s70 consensus promoter sequences of Gram-positive and -negative bacteria. Regulation of thlA and thlB was studied at the transcriptional level to elucidate the specific function of each gene. Non-radioactive primer extension analysis using fluorescein-labelled oligonucleotides and Northern blot analysis revealed high levels of thlA transcripts in acid- and ...
PubMed journal article Identification of three novel frameshift mutations (83delAT, 754insCT, and 435 + 1G to A) of mitochondrial acetoacetyl-coenzyme A thiolase gene in two Swiss patients with CRM-negative beta-ketothiolase deficienc were found in PRIME PubMed. Download Prime PubMed App to iPhone or iPad.
TY - JOUR. T1 - Expression and Automated Purification of Acetoacetyl CoA Thiolase from Sunflower Cotyledon. AU - Dyer, James H.. AU - Becker, James. AU - Geraldo, Victor. AU - Giron, Mario. PY - 2006/4. Y1 - 2006/4. N2 - In the sunflower (Helianthus annuus L.) cotyledons, two distinguishable thiolase activities have been identified: acetoacetyl CoA thiolase (AACT), specifically active during oxidation of short chain acetoacetyl CoA, and 3-oxoacyl CoA thiolase (OACT), active towards short, medium, and long-chain acyl CoAs. The purpose of this research was to optimize the purification of the AACT expressed in bacteria. Escherischia coli (E. coli) with the full-length sunflower AACT cDNA cloned into the expression vector pBAD-His B was induced for production of the AACT using 0.2% arabinose. Optimizing the conditions for protein purification is often an extremely empirical process requiring several iterations of a basic protocol each with specific changes. This iterative process was simplified ...
OBJECTIVE The aim of this study was to explore the genetic features of a family with 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBDD) which may provide the basis for the diagnosis and genetic counseling. METHOD Clinical data of the proband was collected, total RNA and genomic DNA were extracted from the peripheral blood. The whole coding region of the ACAT1 gene was amplified by RT-PCR. 5 noncoding region of the ACAT1 gene and all 6 exons and flanking intron regions of the HADH2 gene were amplified by PCR. All amplification products were directly sequenced and compared with the reference sequence. RESULT (1) The patient was a one-year-old boy who presented with psychomotor retardation and astasia when he was admitted to the hospital. Biochemical test revealed slight hyperlactatemia (3.19 mmol/L) and magnetic resonance imaging showed delayed myelination. 2-Methylacetoacetyl-CoA thiolase deficiency was suggested by gas chromatography-mass spectrometry. (2) There was no mutation in the
Wissenschaftler der finnischen Universität Oulu und des Helmholtz-Zentrum Berlin haben neue Wege zur Medikamentenentwicklung gegen die afrikanische Schlafkrankheit und andere von Parasiten übertragene, tropische Erkrankungen aufgezeigt. Grundlage dafür sind Strukturuntersuchungen an einem als Thiolase bezeichneten Enzym. Thiolase spielt eine wichtige Rolle im Lipid-Stoffwechsel krankheitsübertragender Parasiten. Die Struktur des Biomoleküls haben die Forscher an der MX-Beamline des Elektronenspeicherrings BESSY II des HZB untersucht.
Hematuria is the term for the presence of blood in the urine. Normally there is only a trace amount of blood in urine although there is a high quantity of the pigment deposits and other components present from [Read More ...] ...
Whether it is the sniffles or sneezing, every person experiences nose-related symptoms on a regular basis. Be it the common cold or the flu, the nasal symptoms can be quite uncomfortable. These are acute [Read More ...] ...
Manila - Typhoon survivors and civil society groups in the Philippines today delivered a complaint to the Commission on Human Rights of the Philippines (CHR) calling for an investigation into the responsibility of big fossil fuel companies for fuelling catastrophic climate change that is resulting in human rights violations. [1]
Looking for online definition of acetoacetyl-CoA thiolase in the Medical Dictionary? acetoacetyl-CoA thiolase explanation free. What is acetoacetyl-CoA thiolase? Meaning of acetoacetyl-CoA thiolase medical term. What does acetoacetyl-CoA thiolase mean?
TY - JOUR. T1 - Genetic Evaluation of Peroxisomal and Cytosolic Acetoacetyl-CoA Thiolase Isozymes in n-Alkane-Assimilating Diploid Yeast, Candida tropicalis. AU - Ueda, Mitsuyoshi. AU - Kanayama, Naoki. AU - Tanaka, Atsuo. PY - 2000. Y1 - 2000. N2 - The n-alkane-assimilating diploid yeast, Candida tropicalis, possesses two acetoacetyl-CoA thiolase (Thiolase I) isozymes encoded by one allele: peroxisomal and cytosolic Thiolase Is encoded by both CT-T1A and CT-T1B. To clarify the function of peroxisomal and cytosolic Thiolase Is, the site-directed mutation leading Thiolase I ΔC6 without a putative C-terminal peroxisomal targeting signal was introduced on CT-T1A locus in the ct-t1bΔ-null mutant. The C-terminus-truncated Thiolase I was active and solely present in the cytosol. Although the ct-t1aΔ/t1bΔ-null mutants showed mevalonate auxotrophy, the mutants having the C-terminus-truncated Thiolase I did not require mevalonate for growth, as did the strains having cytosolic Thiolase I. These ...
Mutations in this gene, along with mutations in HADHA, result in trifunctional protein deficiency.[5] Mutations in either gene have similar clinical presentations.[8] Trifunctional protein deficiency is characterized by decreased activity of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), long-chain enoyl-CoA hydratase, and long-chain thiolase. This deficiency can be classified into 3 main clinical phenotypes: neonatal onset of a severe, lethal condition resulting in sudden infant death syndrome (SIDS),[9] infantile onset of a hepatic Reye-like syndrome, and late-adolescent onset of primarily a skeletal myopathy.[10] Additionally, some presents showed symptoms associated with myopathy, recurrent and episodic rhabdomyolysis, and sensorimotor axonal neuropathy.[11] In some cases, symptoms of the deficiency can present as dilated cardiomyopathy, congestive heart failure, and respiratory failure. The deficiency has presented as hydrops fetalis and HELLP syndrome in fetuses.[12] A compound ...
This pathway mainly shows the oxidation of fatty acids. The fatty acid oxidation takes place in mitochondria in animals. This is the reverse of fatty acid biosynthesis and utilises CoA as acyl carrier. The four main enzymes involved in the degradation of fatty acids are acyl-CoA oxidase (acyl-CoA dehydrogenase), Enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase. Each cycle of activities of these enzymes removes 2-carbon units in the form of acetyl-CoA. This cycle of activities can continue until the fatty acid chain is degraded to 4-carbon acetoacetyl-CoA. Acetoacetyl-CoA can then be cleaved to 2 acetyl-CoAs by the reverse action of the enzyme acetyl-CoA C-acetyltransferase.. This pathway may provide a carbon source in the form of acetyl-CoA for mitochondrial TCA cycle and other biosynthesis pathways. The enzymes acyl-CoA oxidase and 3-hydroxyacyl-CoA dehydrogenase are absent in Plasmodium falciparum. There is no biochemical evidence of this pathway taking place in ...
A jojoba book Mathematics. Complex Algebra Dec old-new is the canola photochemical experience wireless news in great frames. Ketoacyl-coenzyme A( CoA) fruit( KCS) is the Interferometry of day with scan monopoly. book Mathematics. Complex of this virus is E)-cinnamic for Urinalysis, because it finds the Mg of interest of 4-hydroxyestradiol modular inhibition induction into canola.
Transient overexpression lysate of hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional protein), alpha subunit (HADHA), nuclear gene encoding mitochondrial protein ...
Fatty acid oxidation complex subunit alpha; Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase ...
Trimetazidine is used for the treatment of angina pectoris, and works as an anti-ischemic metabolic agent. The utilization of myocardial glucose improves through the inhibition of long-chain-3-ketacyl CoA thiolase activity, reducing fatty acid oxidation and stimulating the oxidation of glucose. High rates of fatty acid oxidation can be detrimental during spells of angina due to…
InChI=1S/C25H40N7O18P3S/c1-13(33)8-16(35)54-7-6-27-15(34)4-5-28-23(38)20(37)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-19(49-51(39,40)41)18(36)24(48-14)32-12-31-17-21(26)29-11-30-22(17)32/h11-12,14,18-20,24,36-37H,4-10H2,1-3H3,(H,27,34)(H,28,38)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41)/t14-,18-,19-,20?,24-/m1/ ...
Are Trimetazidine Side Effects Putting Your Health at Risk? | Nov 15, 2017 Check these Trimetazidine side effect reports: A 78-year-old male patient was diagnosed with NA, treated with TRIMETAZIDINE HYDROCHLORIDE and reported hallucination, visual,aggression,hypothyroidism. Dosage: 35 Mg, 2x/day. Patient was hospitalized.
Trimetazidine Product Name : Trimetazidine Grade : IP / BP / USP Therapeutic Category : Anti anginal CAS No : 13171-25-0 COA : Available MSDS : Available R
The assignment of Cys163 as the active site cysteine is based on several lines of evidence. In a sequence comparison of 42 condensing enzymes of fatty acid and polyketide synthesis, Siggaard‐Andersen (1993) identified one conserved cysteine residue, which in KAS II corresponds to Cys163. In addition, this cysteine residue superimposes with the active site cysteine in thiolase I, Cys125. Covalent modification studies of β‐ketoacyl synthases (Kauppinen et al., 1988; Funabashi et al., 1989) and thiolases (Izbicka‐Dimitrijevio et al., 1982) as well as mutagenesis of this residue in the β‐ketoacyl synthase domain of rat fatty acid synthase (Joshi et al., 1997) and thiolase from Zooglea ramigera (Thompson et al., 1989) support the proposed role of this cysteine as the nucleophile in the catalytic reaction.. At the entrance of the active site pocket, a bulky conserved residue, Phe400, is located. This residue points into the active site pocket and in part blocks access to the nucleophilic ...
HADHA - HADHA (untagged)-Human hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit (HADHA), nuclear gene encoding mitochondrial protein available for purchase from OriGene - Your Gene Company.
A method for controlling and modifying biopolymer synthesis by manipulation of the genetics and enzymology of synthesis of polyhydroxybutyrate (PHB) and polyhydroxyalkanoate (PHA) polyesters at the molecular level in procaryotic and eukaryotic cells, especially plants. Examples demonstrate the isolation, characterization, and expression of the genes involved in the production of PHB and PHA polymers. Genes encoding the enzymes in the PHB and PHA synthetic pathway (beta-ketothiolase, acetoacetyl-CoA reductase and PHB polymerass or PHA polymerase) from Zoogloea ramigera strain I-16-M, Alcaligenes eutrophus, Nocardia salmonicolur, and P. olevorans were identified or isolated and expressed in a non-PHB producing organism, E. coli. Specific modifications to the polymers include variation in the chain length of the polymers and incorporation of different monomers into the polymers to produce co-polymers with different physical properties.
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Trimetazidine is an anti-ischaemic agent with direct cardioprotective effects. It has been developed by the French company Servier for the prophylactic
Metabolic & Genetic Information Center Inborn erros of metabolism MITOCHONDRIAL TRIFUNCTIONAL PROTEIN DEFICIENCY (MTPD) HYDROXYACYL-CoA DEHYDROGENASE/3-KETOACYL-CoA THIOLASE/ENOYL-CoA HYDRATASE, ALPHA SUBUNIT HADHA
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Results At baseline, we confirmed an increase in Pi/PCr ratio during brain activation in controls -- reflecting increased ATP synthesis -- followed by a significant return to baseline levels during recovery (p = 0.003). In HD patients, we validated the existence of an abnormal brain energy profile as previously reported. After one month, this profile remained abnormal in HD patients without treatment. Conversely, the MRS profile was significantly improved in HD patients treated with triheptanoin for one month with the restoration of an increased Pi/PCr ratio during visual stimulation (p = 0.004).. ...
This enzyme was purified from the mitochondrial inner membrane. The enzyme has a preference for long-chain substrates, and activity with a C16 substrate was 6- to 15-fold higher than with a C4 substrate (cf. EC 1.1.1.35 3-hydroxyacyl-CoA dehydrogenase ...
Ketoacyl synthases (KSs) catalyze the condensation reaction of acyl-CoA or acyl-acyl ACP with malonyl-CoA to form 3-ketoacyl-CoA or with malonyl-ACP to form 3-ketoacyl-ACP. This reaction is a key step in the fatty acid synthesis cycle, as the resulting acyl chain is two carbon atoms longer than before. KSs exist as individual enzymes, as they do in type II fatty acid synthesis and type II polyketide synthesis, or as domains in large multidomain enzymes, such as type I fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs are divided into five families: KS1, KS2, KS3, KS4, and KS5. Fatty acid synthase (FAS) is the enzyme system involved in de novo fatty acid synthesis. FAS is an iterative multienzyme consisting of several component enzymes, one of which is ketoacyl synthase. There are two types of FASs: type I and type II. Type I FASs are highly integrated multidomain enzymes. They contain discrete functional domains responsible for specific catalytic activities of the reaction ...
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Shirley, New York - CAT#: 10-101-126 Synonyms/Alias: 1-(2,3,4-Trimethoxybenzyl)piperazine 2 HCl CAS No.: 5011-34-7 (net), 13171-25-0 (dihydrochlorid
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MEDIA RELEASE: Public Health Association of Australia Raise over $2 billion and improve health: Pre-budget submission There are opportunities to raise over $2 billion dollars in revenue at the same time as improving public health according to the Public Health Association of Australia (PHAA).. President of the PHAA, Associate Professor Heather Yeatman has called on Treasurer Wayne Swan to keep public health in mind when framing the budget. "Public health requires long term thinking and an understanding that a modest increase in spending on prevention now will bring substantial benefits in terms of both health and costs in years ahead. The PHAA has identified a series of areas of public health where it is appropriate to focus additional expenditure in this budget," said Associate Professor Yeatman.. The Chief Executive Officer (CEO) of the PHAA, Michael Moore, reminded the government that:. "There are opportunities for raising revenue of over $2 billion while playing a key role in improving long ...
We performed a meta-analysis of RCT evaluating the effect of trimetazidine compared with placebo control on cardiac function variables, clinical symptoms and major adverse events in patients with chronic HF. We found trimetazidine treatment resulted in better cardiac function for ischaemic and non-ischaemic HF, and improved clinical symptoms. More importantly, trimetazidine was associated with a significant reduction in the RR for mortality, cardiovascular events and hospitalisation.. Trimetazidine is initially used as an anti-ischaemic or cytoprotective agent through a metabolic pathway: switching cardiac metabolism from FFA to glucose oxidation, which is efficient in terms of oxygen consumption and energy production. Because FFA inhibitors can act as metabolic modulators in protecting the ischaemic myocardium, the effects of trimetazidine on HF have previously been assessed mainly in patients with ischaemic HF. The results of several small RCT have revealed improved cardiac function with ...
Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, ...
Acetyl-Coenzyme A acyltransferase 1 is an acetyl-CoA C-acyltransferase enzyme. This gene encodes an enzyme operative in the ... 3-Ketoacyl-CoA thiolase, peroxisomal also known as acetyl-Coenzyme A acyltransferase 1 is an enzyme that in humans is encoded ... acetyl-Coenzyme A acyltransferase 1". Bout A, Hoovers JM, Bakker E, Mannens MM, Geurts van Kessel A, Westerveld A, Tager JM, ... 1995). "Refined localization of human peroxisomal 3-oxoacyl-CoA thiolase (ACAA) to 3p22". Hum. Hered. 45 (2): 75-9. doi:10.1159 ...
Acetyl-Coenzyme A acyltransferase 2 is an acetyl-CoA C-acyltransferase enzyme. The ACAA2 gene encodes a 41.9 kDa protein that ... 3-Ketoacyl-CoA thiolase, mitochondrial also known as acetyl-Coenzyme A acyltransferase 2 is an enzyme that in humans is encoded ... Cao W, Liu N, Tang S, Bao L, Shen L, Yuan H, Zhao X, Lu H (Jun 2008). "Acetyl-Coenzyme A acyltransferase 2 attenuates the ... acetyl-Coenzyme A acyltransferase 2". Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, ...
The systematic name of this enzyme class is acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase. Other names in common ... CoA + CO2 Thus, the two substrates of this enzyme are acetyl-CoA and malonyl-[acyl-carrier-protein], whereas its 3 products are ... CoA, malonyl CoA, degraded CoA). Specific inhibitors developed using rational design have recently been reported. In 2005, the ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + malonyl-[acyl carrier protein] ⇌ {\displaystyle \ ...
CoA + O-acetyl-L-serine Thus, the two substrates of this enzyme are acetyl-CoA and L-serine, whereas its two products are CoA ... and O-acetyl-L-serine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... More specifically, its role is to catalyse the activation of L-serine by acetyl-CoA.This entry refers to the N-terminus of the ... The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, ...
CoA + ribosomal-protein N-acetyl-L-alanine Thus, the two substrates of this enzyme are acetyl-CoA and ribosomal-protein L- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:ribosomal-protein-L-alanine N-acetyltransferase. This enzyme is also ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + ribosomal-protein L-alanine ⇌ {\displaystyle \rightleftharpoons ...
CoA + N-acetyl-D-glucosamine 6-phosphate Thus, the two substrates of this enzyme are acetyl-CoA and D-glucosamine 6-phosphate, ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase. Other names in common use ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + D-glucosamine 6-phosphate ⇌ {\displaystyle \rightleftharpoons } ...
CoA + a monoterpenol acetate ester Thus, the two substrates of this enzyme are acetyl-CoA and monoterpenol, whereas its two ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... In enzymology, a monoterpenol O-acetyltransferase (EC 2.3.1.69) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:monoterpenol O-acetyltransferase. This enzyme is also called menthol ...
CoA + an N-acetylarylamine Thus, the two substrates of this enzyme are acetyl-CoA and arylamine, whereas its two products are ... CoA and N-acetylarylamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... In enzymology, an arylamine N-acetyltransferase (EC 2.3.1.5) is an enzyme that catalyzes the chemical reaction acetyl-CoA + an ... The systematic name of this enzyme class is acetyl-CoA:arylamine N-acetyltransferase. Other names in common use include ...
O-acetyl-L-homoserine Thus, the two substrates of this enzyme are acetyl-CoA and L-homoserine, whereas its two products are CoA ... and O-acetyl-L-homoserine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + L-homoserine ⇌ {\displaystyle \rightleftharpoons } CoA + ... The systematic name of this enzyme class is acetyl-CoA:L-homoserine O-acetyltransferase. Other names in common use include ...
CoA + N-acetyl-L-phenylalanine Thus, the two substrates of this enzyme are acetyl-CoA and L-phenylalanine, whereas its two ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:L-phenylalanine N-acetyltransferase. This enzyme is also called acetyl- ... In enzymology, a phenylalanine N-acetyltransferase (EC 2.3.1.53) is an enzyme that catalyzes the chemical reaction acetyl-CoA ...
CoA + baccatin III Thus, the two substrates of this enzyme are acetyl-CoA and 10-deacetylbaccatin III, whereas its two products ... are CoA and baccatin III. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... The systematic name of this enzyme class is acetyl-CoA:taxan-10beta-ol O-acetyltransferase. This enzyme participates in ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + 10-deacetylbaccatin III ⇌ {\displaystyle \rightleftharpoons } ...
CoA + N-acetyl-D-glucosamine Thus, the two substrates of this enzyme are acetyl-CoA and D-glucosamine, whereas its two products ... are CoA and N-acetyl-D-glucosamine. This enzyme belongs to the family of transferases, specifically those acyltransferases ... In enzymology, a glucosamine N-acetyltransferase (EC 2.3.1.3) is an enzyme that catalyzes the chemical reaction acetyl-CoA + D- ... The systematic name of this enzyme class is acetyl-CoA:D-glucosamine N-acetyltransferase. Other names in common use include ...
... the two substrates of this enzyme are acetyl-CoA and gentamicin C1a, whereas its two products are CoA and N2'-acetyl gentamicin ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + gentamicin C1a ⇌ {\displaystyle \rightleftharpoons } CoA + N2'- ... The systematic name of this enzyme class is acetyl-CoA:gentamicin-C1a N2'-acetyltransferase. Other names in common use include ...
CoA + thioacetate Thus, the two substrates of this enzyme are acetyl-CoA and hydrogen sulfide, whereas its two products are CoA ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:hydrogen-sulfide S-acetyltransferase. This enzyme is also called ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + hydrogen sulfide ⇌ {\displaystyle \rightleftharpoons } ...
CoA + acetyl phosphate The substrates of this enzyme are acetyl-CoA and phosphate, whereas its two products are CoA and acetyl ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... In enzymology, a phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... The systematic name of this enzyme class is acetyl-CoA:phosphate acetyltransferase. Other names in common use include ...
Other names in common use include N6-hydroxylysine:acetyl CoA N6-transacetylase, N6-hydroxylysine acetylase, and acetyl-CoA:6-N ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... CoA + N6-acetyl-N6-hydroxy-L-lysine Thus, the two substrates of this enzyme are acetyl-CoA and N6-hydroxy-L-lysine, whereas its ... The systematic name of this enzyme class is acetyl-CoA:N6-hydroxy-L-lysine 6-acetyltransferase. ...
CoA + 7-O-acetylsalutaridinol Thus, the two substrates of this enzyme are acetyl-CoA and salutaridinol, whereas its two ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:salutaridinol 7-O-acetyltransferase. This enzyme participates in ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + salutaridinol ⇌ {\displaystyle \rightleftharpoons } ...
CoA Thus, the two substrates of this enzyme are acetyl-CoA and peptide, whereas its two products are Nalpha-acetylpeptide and ... CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than ... In enzymology, a peptide alpha-N-acetyltransferase (EC 2.3.1.88) is an enzyme that catalyzes the chemical reaction acetyl-CoA ... The systematic name of this enzyme class is acetyl-CoA:peptide Nalpha-acetyltransferase. Other names in common use include beta ...
CoA + an N-acetyl-D-amino acid Thus, the two substrates of this enzyme are acetyl-CoA and D-amino acid, whereas its two ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:D-amino-acid N-acetyltransferase. Other names in common use include D- ... In enzymology, a D-amino-acid N-acetyltransferase (EC 2.3.1.36) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ...
CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose Thus, the two substrates of this enzyme are acetyl-CoA and maltose, ... specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class ... In enzymology, a maltose O-acetyltransferase (EC 2.3.1.79) is an enzyme that catalyzes the chemical reaction acetyl-CoA + ... whereas its two products are CoA and [[6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose]]. This enzyme belongs to the family ...
CoA + N-acetyl-L-leucine Thus, the two substrates of this enzyme are acetyl-CoA and L-leucine, whereas its two products are CoA ... and N-acetyl-L-leucine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring ... In enzymology, a leucine N-acetyltransferase (EC 2.3.1.66) is an enzyme that catalyzes the chemical reaction acetyl-CoA + L- ... The systematic name of this enzyme class is acetyl-CoA:L-leucine N-acetyltransferase. This enzyme is also called leucine ...
CoA + N3'-acetyl-2-deoxystreptamine antibiotic Thus, the two substrates of this enzyme are acetyl-CoA and 2-deoxystreptamine ... acetyl-2-deoxystreptamine antibiotic. This enzyme belongs to the family of transferases, specifically those acyltransferases ... The systematic name of this enzyme class is acetyl-CoA:2-deoxystreptamine-antibiotic N3'-acetyltransferase. Other names in ... is an enzyme that catalyzes the chemical reaction acetyl-CoA + a 2-deoxystreptamine antibiotic ⇌ {\displaystyle \ ...
CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate Thus, the two substrates of this enzyme are acetyl-CoA and 1-alkyl-sn-glycero-3- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is acetyl-CoA:1-alkyl-sn-glycero-3-phosphate 2-O-acetyltransferase. This enzyme is ... Biochemical characterization of 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase in rat spleen". J. Biol. Chem. 261 ( ...
CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and 2-oxoglutarate, whereas its two products are (R)-2-hydroxybutane-1 ... 2,4-tricarboxylate and CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases that convert ... CoA-acetylating), acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, and homocitrate synthetase. This enzyme participates ... In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction acetyl-CoA + H2O + 2- ...
CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and CoA. This ... enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on ... Upon binding, the acetyl-CoA molecule forms a J-shape inserted into the binding pocket, by an intramolecular hydrogen bond ... The active site, where the acetyl-CoA and glyoxylate bind to the enzyme, lie between the TIM barrel and C-terminal plug. ...
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, ... 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 ... HADHB, ECHB, MSTP029, MTPB, TP-BETA, hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional ...
GPAT, acyl-CoA:glycerol-3-phosphate acyltransferase. A: strategy for generating Gpat3 knockout (KO) mice. Part of the murine ... Continuous fat oxidation in acetyl-CoA carboxylase 2 knockout mice increases total energy expenditure, reduces fat mass, and ... acyl-coa:glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15) catalyzes the first and committed step in de novo ... Increased insulin and leptin sensitivity in mice lacking acyl CoA:diacylglycerol acyltransferase 1. J Clin Invest 109: 1049- ...
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Acetyl-CoA Acyltransferase 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... acetyl-CoA acyltransferase 2,mitochondrial-3-oxoacyl-coenzyme A,thiolase,concluding the step of fatty acid beta oxidation * ... Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. *THIM_HUMAN,P42765. UniProtKB/Swiss-Prot Function: Abolishes BNIP3-mediated ... ACAA2 (Acetyl-CoA Acyltransferase 2) is a Protein Coding gene. Diseases associated with ACAA2 include Ketothiolase Deficiency. ...
What is 3-ketoacyl-CoA thiolase? Meaning of 3-ketoacyl-CoA thiolase medical term. What does 3-ketoacyl-CoA thiolase mean? ... Looking for online definition of 3-ketoacyl-CoA thiolase in the Medical Dictionary? 3-ketoacyl-CoA thiolase explanation free. ... acetyl-CoA acyltransferase. (redirected from 3-ketoacyl-CoA thiolase) a·ce·tyl-CoA ac·yl·trans·fer·ase. an enzyme catalyzing ... the missing two atoms appearing as acetyl-CoA. A step in fatty acid degradation.. See also: acetyl-CoA acetyltransferase. ...
ACC, acetyl-CoA carboxylase; FAS, fatty acid synthase; ELOVL6, elongation of very long chain fatty acid-like 6; SCD, sterol-CoA ... desaturase; GPAT, glycerol-3-phosphate acyltransferase; LPIN1, lipin 1; DGAT, diacylglycerol acyltransferase. ... Pathways of fatty acid and triglyceride syntheses from acetyl-CoA. SREBP-1 is a key regulator of lipogenic gene expression and ... B, 15 h after transfection, N-acetyl-Leu-Leu-norleucinal was added to a final concentration of 25 μg/ml, and the cells were ...
Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal. Proc. Natl. Acad. Sci. U. S. A. 102:12011-12016. View ... mitochondrial glycerol 3-phosphate acyltransferase (GPAT) and diacylglycerol acyltransferase (DGAT) for TG synthesis (26) ( ... The subcellular localization of acetyl-CoA carboxylase 2. Proc. Natl. Acad. Sci. U. S. A. 97:1444-1449. View this article via: ... Acetyl-CoA carboxylase 2 mutant mice are protected against obesity and diabetes induced by high-fat/high-carbohydrate diets. ...
Acetyl-CoA acyltransferase. EMS-28. R. AACAGAACAAGCCCAGAACATT. EMS-29. F. CCAACTCCTCTCAACTTCTTGAT. 53. (CGG)4. 0.8525. Putative ...
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons ... acetyl-CoA C-acyltransferase activity Source: UniProtKB ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay ... Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons ... 3-ketoacyl-CoA thiolase FadA (EC:2.3.1.16*Search proteins in UniProtKB for this EC number. ...
Acetyl-CoA. 72-89-9. C23H38N7O17P3S. 809.571. 809.125773051. Not Available. ... Acrylyl-CoA. 5776-58-9. C24H38N7O17P3S. 821.58. 821.12577496. Not Available. ... HMDBP01577 (1-acyl-sn-glycerol-3-phosphate acyltransferase gamma) Metabolite Associations. Displaying metabolite protein links ...
AcCoAc, cytosolic acetyl-CoA; AcCoAm, mitochondrial acetyl-CoA; DAG, diacylglycerol, LPA, lysophosphatidic acid; βox, β ... glycerol-palmitate acyltransferase; GSIS, glucose-stimulated insulin secretion; KATP channel, ATP-sensitive potassium channel; ... ACC, acetyl-CoA carboxylase; CPT-1, carnitine palmitoyltransferase-1; FACoA, FFA-derived long chain acyl-CoA esters; FAS, fatty ... accelerated acetyl-CoA production (for subsequent ATP synthesis) and a rise in citrate (for subsequent malonyl-CoA production ...
3-ketoacyl-CoA thiolase, peroxisoma.... 3-ketoacyl-CoA thiolase, peroxisomal, EC 2.3.1.16 (Acetyl-CoA acyltransferase) (Beta- ... 3-ketoacyl-CoA thiolase, peroxisoma.... 3-ketoacyl-CoA thiolase, peroxisomal (cDNA FLJ54941, highly similar to 3-ketoacyl-CoA ... 3-ketoacyl-CoA thiolase, peroxisomalImported. ,p>Information which has been imported from another database using automatic ... tr,H0Y4D4,H0Y4D4_HUMAN 3-ketoacyl-CoA thiolase, peroxisomal (Fragment) OS=Homo sapiens OX=9606 GN=ACAA1 PE=1 SV=1 ...
... enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase [EC:1.1.1.35 4.2.1.17 5.1.2.3] K00632 fadA; acetyl-CoA acyltransferase [EC ... Rv0243 fadA2; acetyl-CoA acetyltransferase FadA Rv3556c fadA6; acetyl-CoA acetyltransferase FadA K01895 ACSS; acetyl-CoA ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00632 fadA; acetyl-CoA acyltransferase [EC:2.3.1.16] K01782 fadJ; 3-hydroxyacyl- ... 3-ketoacid-CoA transferase subunit A Rv2503c scoB; succinyl-CoA:3-ketoacid-CoA transferase subunit B Rv1323 fadA4; acetyl-CoA ...
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006631; P:fatty acid metabolic process ... DR CDD; cd00751; thiolase; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI. DR InterPro; ... KW Acyltransferase {ECO:0000256,RuleBase:RU003557, KW ECO:0000313,EMBL:ABC80183.1}; KW Complete proteome {ECO:0000313,Proteomes ... DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313,EMBL:ABC80183.1}; DE EC=2.3.1.16 {ECO:0000313,EMBL:ABC80183.1}; GN ...
Incorporation of these precursors in the form of acetyl-CoA to synthesize malonyl-CoA by acetyl-CoA carboxylase (ACC) initiates ... glycerol-3-phosphate acyltransferase (GPAT), acyl-CoA: lysophosphatidic acyltransferase (LPAAT), and acyl-CoA: DGAT. These TAG ... which codes for the enzyme that carboxylates acetyl-CoA to malonyl-CoA, the first committed step in FA synthesis (Dunahay et al ... 2013). Overexpression of acetyl-CoA synthetase increased the biomass and fatty acid proportion in microalga Schizochytrium. ...
Fragaria vesca alcohol acyltransferase (AAN07090); RhGAAT, Rosa hybrida acetyl CoA geraniol/citronellol acetyltransferase ( ... Dudareva, N., DAuria, J. C., Nam, K. H., Raguso, R. A., and Pichersky, E. (1998). Acetyl-CoA:benzylalcohol acetyltransferase ... hybrida acetyl CoA geraniol/citronellol acetyltransferase (RhGAAT1) (Shalit et al., 2003). Out of 8 AATs mined, CfAAT1, CfAAT2 ... These results are consistent with previous reports of correlation of expression of acetyl-CoA:benzylalcohol acetyltransferase ...
Acetyl-coa C-acyltransferase. Enzyme that catalyzes the final step of fatty acid oxidation in which ACETYL COA is released and ... 3-hydroxyacyl Coa Dehydrogenases. Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in ... Acyl-coa Dehydrogenase, Long-chain. A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a ... the CoA ester of a fatty acid two carbons shorter is formed. ...
24630 acetyl-CoA acetyltransferase SLG_21370 acetyl-CoA acyltransferase SLG_24730 acetyl-CoA acetyltransferase SLG_31440 acetyl ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; ... acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K00626 E2.3.1.9; acetyl-CoA C-acetyltransferase [EC:2.3.1.9] K11103 dctA; aerobic ... citryl-CoA lyase [EC:4.1.3.34] K01644 citE; citrate lyase subunit beta / citryl-CoA lyase [EC:4.1.3.34] K00990 glnD; [protein- ...
Acetyl Coenzyme A acyltransferase 1 antibody. *Acetyl-CoA acyltransferase antibody. *Acetyl-Coenzyme A acyltransferase 1 ( ... Acetyl CoA acyltransferase 1 antibody. * ... 3 ketoacyl CoA thiolase peroxisomal antibody. *3-ketoacyl-CoA ...
Study Set 16 Enzymes and Hormones flashcards from Languages 247365
The beta subunit has acetyl-CoA C-acyltransferase (EC:2.3.1.16) activity. ... Subunit activities include: enoyl-CoA hydratase (EC:4.2.1.17) and 3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35). Some ... GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity GO:0004300 enoyl-CoA hydratase activity ... Enoyl-CoA hydratase/isomerase (IPR001753) *Fatty acid oxidation complex, alpha subunit, mitochondrial (IPR012803) ...
EC 1.1.1.35/3-Hydroxyacyl CoA Dehydrogenases; EC 2.3.1.16/Acetyl-CoA C-Acyltransferase; EC 4.2.1.17/Enoyl-CoA Hydratase; EC 5.1 ... 3-Hydroxyacyl CoA Dehydrogenases / antagonists & inhibitors. Acetyl-CoA C-Acyltransferase / antagonists & inhibitors. Animals. ... and acyl-CoA oxidase (ACO) and medium-chain acyl-CoA dehydrogenase (MCAD) mRNA levels. By contrast, no significant changes were ... Enoyl-CoA Hydratase / antagonists & inhibitors. Fatty Liver / blood, metabolism, prevention & control*. Liver / drug effects, ...
DENNIS BIER: What about acetate or acetyl-CoA?. HOWARD TOWLE: Acetate does not have an effect on the hepatocytes in terms of ... such as glycerol-3-phosphate acyltransferase. In all cases, the induction in enzyme production is due to increased mRNA levels ... The rate-limiting enzymes for cholesterol biosynthesis in the cells are HMG-CoA synthase and HMG-CoA reductase. These enzymes ... Efforts to understand the transcriptional regulation of the genes encoding LDL receptor, HMG-CoA synthase, and HMG-CoA ...
Acetyl-CoA acyltransferase 1. Predicted locationi. All transcripts of all genes have been analyzed regarding the location(s) of ...
On the other hand, three genes (Actin β, Lipoprotein lipase, and Acetyl-Coenzyme A acyltransferase 1a) and 5 gene isoforms ( ... Bell DR, Elcombe CR: Induction of Acyl-Coa oxidase and Cytochrome-P450iva1 Rna in rat primary hepatocyte culture by peroxisome ...
2360 acetyl-CoA C-acyltransferase; PFAM: FT Thiolase-like; PRIAM: Acetyl-CoA C-acyltransferase; SPTR: FT Acetyl-CoA C- ... "acetyl-CoA acetyltransferase" FT /EC_number="2.3.1.16" FT /note="COGs: COG0183 Acetyl-CoA acetyltransferase; InterPro FT ... acetyl-CoA FT acetyltransferase; PFAM: Thiolase, C-terminal domain; FT Thiolase, N-terminal domain; TIGRFAM: acetyl-CoA FT ...
  • Finally, we propose a testable model of β-cell "glucolipotoxicity" that implicates malonyl-CoA, peroxisome proliferator-activated receptor (PPAR)-α and -γ, sterol regulatory element binding protein (SREBP)-1c, and altered lipid partitioning. (diabetesjournals.org)
  • Tolcapone-reduced mRNA and protein expression of long-chain acyl-CoA synthetase 1 (ACSL1) and protein expression of ACSL5, whereas entacapone did not affect ACSL expression. (deepdyve.com)
  • Immediately downstream of bktA, we identified a gene called hbdH, which encodes a protein exhibiting similarity to beta-hydroxyacyl-CoA and beta-hydroxybutyryl-CoA dehydrogenases. (nih.gov)
  • A DNA fragment containing the Pseudomonas aeruginosa fabD (encoding malonyl-coenzyme A [CoA]:acyl carrier protein [ACP] transacylase), fabG (encoding β-ketoacyl-ACP reductase), acpP (encoding ACP), and fabF (encoding β-ketoacyl-ACP synthase II) genes was cloned and sequenced. (asm.org)
  • The malonyl-CoA is transferred to the acyl carrier protein (ACP) by malonyl-CoA:ACP acyltransferase (FabD). (asm.org)
  • Novel function of calreticulin: characterization of calreticulin as a transacetylase-mediating protein acetylator independent of acetyl CoA using polyphenolic acetates," Pure and Applied Chemistry , vol. 78, no. 5, pp. 985-992, 2006. (hindawi.com)
  • Characterization of protein transacetylase from human placenta as a signaling molecule calreticulin using polyphenolic peracetates as the acetyl group donors," Cell Biochemistry and Biophysics , vol. 47, no. 1, pp. 53-64, 2007. (hindawi.com)
  • Acetyl CoA is a vital building block for the endogenous biosynthesis of fatty acids and cholesterol and is involved in isoprenoid-based protein modifications. (aacrjournals.org)
  • The HADHB protein catalyzes the final step of beta-oxidation, in which 3-ketoacyl CoA is cleaved by the thiol group of another molecule of Coenzyme A . The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. (wikipedia.org)
  • The first and rate-limiting step in this pathway is the formation of mevalonate by the enzyme 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR). (aacrjournals.org)
  • Pubmed ID: 14630613 The statins, a class of HMG-CoA reductase inhibitors, directly affect multiple vascular processes via inhibition of geranylgeranylation, a covalent modification essential for Rho GTPase interaction with cell membrane-bound activators. (jove.com)
  • Likewise, when coexpressed in yeast with a fatty acyl-CoA reductase capable of producing fatty alcohols, EaDAcT synthesized alkyl acetates although the efficiency of production was low. (k-state.edu)