Coenzyme a transferases. Medical search

Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.

Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.

A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.

A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.

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.

A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.

Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.

Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.

A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.

A non-template-directed DNA polymerase normally found in vertebrate thymus and bone marrow. It catalyzes the elongation of oligo- or polydeoxynucleotide chains and is widely used as a tool in the differential diagnosis of acute leukemias in man. EC 2.7.7.31.

Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.

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.

The rate dynamics in chemical or physical systems.

A sulfhydryl compound used to prevent urothelial toxicity by inactivating metabolites from ANTINEOPLASTIC AGENTS, such as IFOSFAMIDE or CYCLOPHOSPHAMIDE.

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.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

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.

Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.

An enzyme that catalyzes the synthesis of geranylgeranyl diphosphate from trans, trans-farnesyl diphosphate and isopentenyl diphosphate.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A phylum of ARCHAEA comprising at least seven classes: Methanobacteria, Methanococci, Halobacteria (extreme halophiles), Archaeoglobi (sulfate-reducing species), Methanopyri, and the thermophiles: Thermoplasmata, and Thermococci.

The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.

A class of enzymes that transfers nucleotidyl residues. EC 2.7.7.

An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

A post-translational modification of proteins by the attachment of an isoprenoid to the C-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol.

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.

A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds.

Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.

A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.

Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.

A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).

A fungal metabolite isolated from cultures of Aspergillus terreus. The compound is a potent anticholesteremic agent. It inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It also stimulates the production of low-density lipoprotein receptors in the liver.

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.

Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.

A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.

Proteins found in any species of bacterium.

Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of PHOSPHORYLASES. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the HEXOSYLTRANSFERASES; PENTOSYLTRANSFERASES; SIALYLTRANSFERASES; and those transferring other glycosyl groups. EC 2.4.

Phosphoric or pyrophosphoric acid esters of polyisoprenoids.

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).

Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.

Enzymes that catalyze the incorporation of deoxyribonucleotides into a chain of DNA. EC 2.7.7.-.

Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.

Proteins prepared by recombinant DNA technology.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.

Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.

The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.

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)

Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.

Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

An enzyme that catalyzes the synthesis of UDPgalactose from UTP and galactose-1-phosphate. It is present in low levels in fetal and infant liver, but increases with age, thereby enabling galactosemic infants who survive to develop the capacity to metabolize galactose. EC 2.7.7.10.

This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).

The sum of the weight of all the atoms in a molecule.

Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.

An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.

A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.

A derivative of LOVASTATIN and potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It may also interfere with steroid hormone production. Due to the induction of hepatic LDL RECEPTORS, it increases breakdown of LDL CHOLESTEROL.

The functional hereditary units of BACTERIA.

The N-acetyl derivative of glucosamine.

The simplest saturated hydrocarbon. It is a colorless, flammable gas, slightly soluble in water. It is one of the chief constituents of natural gas and is formed in the decomposition of organic matter. (Grant & Hackh's Chemical Dictionary, 5th ed)

Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

A cobalt-containing coordination compound produced by intestinal micro-organisms and found also in soil and water. Higher plants do not concentrate vitamin B 12 from the soil and so are a poor source of the substance as compared with animal tissues. INTRINSIC FACTOR is important for the assimilation of vitamin B 12.

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.

Oxidoreductases that are specific for ALDEHYDES.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.

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.

A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17.

Cyclic TETRAPYRROLES based on the corrin skeleton.

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.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

Enzymes that catalyze the transfer of glucose from a nucleoside diphosphate glucose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

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.

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.

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.

Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.

A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)

The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

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)

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

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.

A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.

The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.

Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.

The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.

Established cell cultures that have the potential to propagate indefinitely.

An enzyme that catalyzes the transfer of UMP from UDPglucose to galactose 1-phosphate, forming UDPgalactose and glucose 1-phosphate. Deficiency in this enzyme is the major cause of GALACTOSEMIA. EC 2.7.7.12.

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.

A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.

The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.

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.

Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.

An antitumor antibiotic produced by Streptomyces sparsogenes. It inhibits protein synthesis in 70S and 80S ribosomal systems.

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.

The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.

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.

An enzyme that catalyzes the conversion of 5-phosphoribosyl-1-pyrophosphate and hypoxanthine, guanine, or 6-mercaptopurine to the corresponding 5'-mononucleotides and pyrophosphate. The enzyme is important in purine biosynthesis as well as central nervous system functions. Complete lack of enzyme activity is associated with the LESCH-NYHAN SYNDROME, while partial deficiency results in overproduction of uric acid. EC 2.4.2.8.

Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Enzymes that catalyze the transfer of mannose from a nucleoside diphosphate mannose to an acceptor molecule which is frequently another carbohydrate. The group includes EC 2.4.1.32, EC 2.4.1.48, EC 2.4.1.54, and EC 2.4.1.57.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.

An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.

The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.

Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)

Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.

An enzyme that catalyzes reversibly the transfer of phosphoethanolamine from CDP-ethanolamine to diacylglycerol to yield phosphatidylethanolamine (cephalin) and CMP. The enzyme is found in the endoplasmic reticulum. EC 2.7.8.1.

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.

Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.

Compounds containing the -SH radical.

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.

A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.

A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.

An enzyme that, in the pathway of cholesterol biosynthesis, catalyzes the condensation of isopentenyl pyrophosphate and dimethylallylpyrophosphate to yield pyrophosphate and geranylpyrophosphate. The enzyme then catalyzes the condensation of the latter compound with another molecule of isopentenyl pyrophosphate to yield pyrophosphate and farnesylpyrophosphate. EC 2.5.1.1.

Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.

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)

Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.

Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.

Enzymes that catalyze the first step leading to the oxidation of succinic acid by the reversible formation of succinyl-CoA from succinate and CoA with the concomitant cleavage of ATP to ADP (EC 6.2.1.5) or GTP to GDP (EC 6.2.1.4) and orthophosphate. Itaconate can act instead of succinate and ITP instead of GTP.EC 6.2.1.-.

Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.

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.

Hydroxycinnamic acid and its derivatives. Act as activators of the indoleacetic acid oxidizing system, thereby producing a decrease in the endogenous level of bound indoleacetic acid in plants.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

A nucleoside diphosphate sugar which serves as a source of N-acetylgalactosamine for glycoproteins, sulfatides and cerebrosides.

7-carbon saturated monocarboxylic acids.

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.

The addition of an organic acid radical into a molecule.

Salts and derivatives of acetoacetic acid.

An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.

The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.

Derivatives of BUTYRIC ACID that include a double bond between carbon 2 and 3 of the aliphatic structure. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include the aminobutryrate structure.

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.

A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.

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.

Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

An essential amino acid that is required for the production of HISTAMINE.

A genus of gram-negative, aerobic, rod-shaped bacteria found in wet soil containing decaying organic material and in water. Cells tend to be pleomorphic if grown on media containing succinate or coccoid if grown in the presence of an alcohol as the sole carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)

Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.

An in situ method for detecting areas of DNA which are nicked during APOPTOSIS. Terminal deoxynucleotidyl transferase is used to add labeled dUTP, in a template-independent manner, to the 3 prime OH ends of either single- or double-stranded DNA. The terminal deoxynucleotidyl transferase nick end labeling, or TUNEL, assay labels apoptosis on a single-cell level, making it more sensitive than agarose gel electrophoresis for analysis of DNA FRAGMENTATION.

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.

A group of inherited enzyme deficiencies which feature elevations of GALACTOSE in the blood. This condition may be associated with deficiencies of GALACTOKINASE; UDPGLUCOSE-HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; or UDPGLUCOSE 4-EPIMERASE. The classic form is caused by UDPglucose-Hexose-1-Phosphate Uridylyltransferase deficiency, and presents in infancy with FAILURE TO THRIVE; VOMITING; and INTRACRANIAL HYPERTENSION. Affected individuals also may develop MENTAL RETARDATION; JAUNDICE; hepatosplenomegaly; ovarian failure (PRIMARY OVARIAN INSUFFICIENCY); and cataracts. (From Menkes, Textbook of Child Neurology, 5th ed, pp61-3)

Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.

A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.

A genus of green nonsulfur bacteria in the family Chloroflexaceae. They are photosynthetic, thermophilic, filamentous gliding bacteria found in hot springs.

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.

The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.

A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.

Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.

Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives.

Proteins found in any species of archaeon.

A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.

A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.

A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.

Enzymes that catalyze the transfer of hydroxymethyl or formyl groups. EC 2.1.2.

The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.

Steroids with a hydroxyl group at C-3 and most of the skeleton of cholestane. Additional carbon atoms may be present in the side chain. (IUPAC Steroid Nomenclature, 1987)

A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.

Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.

Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.

A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

Elements of limited time intervals, contributing to particular results or situations.

A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Biological catalysts and their cofactors.

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (1/146)

The bacterium Sphingomonas sp. strain RW1 is able to use dibenzo-p-dioxin, dibenzofuran, and several hydroxylated derivatives as sole sources of carbon and energy. We have determined and analyzed the nucleic acid sequence of a 9,997-bp HindIII fragment downstream of cistrons dxnA1A2, which encode the dioxygenase component of the initial dioxygenase system of the corresponding catabolic pathways. This fragment contains 10 colinear open reading frames (ORFs), apparently organized in one compact operon. The enzymatic activities of some proteins encoded by these genes were analyzed in the strain RW1 and, after hyperexpression, in Escherichia coli. The first three ORFs of the locus, designated dxnC, ORF2, and fdx3, specify a protein with a low homology to bacterial siderophore receptors, a polypeptide representing no significant homology to known proteins, and a putative ferredoxin, respectively. dxnD encodes a 69-kDa phenol monooxygenase-like protein with activity for the turnover of 4-hydroxysalicylate, and dxnE codes for a 37-kDa protein whose sequence and activity are similar to those of known maleylacetate reductases. The following gene, dxnF, encodes a 33-kDa intradiol dioxygenase which efficiently cleaves hydroxyquinol, yielding maleylacetate, the ketoform of 3-hydroxy-cis,cis-muconate. The heteromeric protein encoded by dxnGH is a 3-oxoadipate succinyl coenzyme A (succinyl-CoA) transferase, whereas dxnI specifies a protein exhibiting marked homology to acetyl-CoA acetyltransferases (thiolases). The last ORF of the sequenced fragment codes for a putative transposase. DxnD, DxnF, DxnE, DxnGH, and DxnI (the activities of most of them have also been detected in strain RW1) thus form a complete 4-hydroxysalicylate/hydroxyquinol degradative pathway. A route for the mineralization of the growth substrates 3-hydroxydibenzofuran and 2-hydroxydibenzo-p-dioxin in Sphingomonas sp. strain RW1 thus suggests itself. (+info)

Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis. (2/146)

The exchange of oxygen atoms between acetate, glutaryl-CoA, and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans was analyzed using [(18)O(2)]acetate together with matrix-assisted laser desorption/ionization time of flight mass spectrometry of an appropriate undecapeptide. The exchange reaction was shown to be site-specific, reversible, and required both glutaryl-CoA and [(18)O(2)]acetate. The observed exchange is in agreement with the formation of a mixed anhydride intermediate between the enzyme and acetate. In contrast, with a mutant enzyme, which was converted to a thiol ester hydrolyase by replacement of the catalytic glutamate residue by aspartate, no (18)O uptake from H(2)(18)O into the carboxylate was detectable. This result is in accord with a mechanism in which the carboxylate of aspartate acts as a general base in activating a water molecule for hydrolysis of the thiol ester intermediate. This mechanism is further supported by the finding of a significant hydrolyase activity of the wild-type enzyme using acetyl-CoA as substrate, whereas glutaryl-CoA is not hydrolyzed. The small acetate molecule in the substrate binding pocket may activate a water molecule for hydrolysis of the nearby enzyme-CoA thiol ester. (+info)

Regulation and adaptation of glucose metabolism of the parasitic protist Leishmania donovani at the enzyme and mRNA levels. (3/146)

Adaptation of the glucose metabolism of Leishmania donovani promastigotes (insect stage) was investigated by simultaneously measuring metabolic rates, enzyme activities, message levels, and cellular parameters under various conditions. Chemostats were used to adapt cells to different growth rates with growth rate-limiting or excess glucose concentrations. L. donovani catabolized glucose to CO(2), succinate, acetate, and pyruvate in ratios that depended on growth rate and glucose availability. Rates of glucose consumption were a linear function of growth rate and were twice as high in excess glucose-grown cells as in glucose-limited organisms. The major end product was CO(2), but organic end products were also formed in ratios that varied strongly with growth conditions. The specific activities of the 14 metabolic enzymes measured varied by factors of 3 to 17. Two groups of enzymes adapted specific activities in parallel, but there was no correlation between the groups. The activities of only one group correlated with specific rates of glucose metabolism. Total RNA content per cellular protein varied by a factor of 6 and showed a linear relationship with the rate of glucose consumption. There was no correlation between steady-state message levels and activities of the corresponding enzymes, suggesting regulation at the posttranscriptional level. A comparison of the adaptation of energy metabolism in L. donovani and other species suggests that the energy metabolism of L. donovani is inefficient but is well suited to the environmental challenges that it encounters during residence in the sandfly, its insect vector. (+info)

Protection of mice against brucellosis by vaccination with Brucella melitensis WR201(16MDeltapurEK). (4/146)

Human brucellosis can be acquired from infected animal tissues by ingestion, inhalation, or contamination of the conjunctiva or traumatized skin by infected animal products. A vaccine to protect humans from occupational exposure or from zoonotic infection in areas where the disease is endemic would reduce an important cause of morbidity worldwide. Vaccines currently used in animals are unsuitable for human use. We tested a live, attenuated, purine-auxotrophic mutant strain of Brucella melitensis, WR201, for its ability to elicit cellular and humoral immune responses and to protect mice against intranasal challenge with B. melitensis 16M. Mice inoculated intraperitoneally with WR201 made serum antibody to lipopolysaccharide and non-O-polysaccharide antigens. Splenocytes from immunized animals released interleukin-2 (IL-2), gamma interferon, and IL-10 when cultured with Brucella antigens. Immunization led to protection from disseminated infection but had only a slight effect on clearance of the challenge inoculum from the lungs. These studies suggest that WR201 should be further investigated as a vaccine to prevent human brucellosis. (+info)

Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase. (5/146)

We have isolated a cDNA clone encoding a mouse haploid germ cell-specific protein from a subtracted cDNA library. Sequence analysis of the cDNA revealed high homology with pig and human heart succinyl CoA:3-oxo acid CoA transferase (EC 2.8.3.5), which is a key enzyme for energy metabolism of ketone bodies. The deduced protein consists of 520 amino acid residues, including glutamate 344, known to be the catalytic residue in the active site of pig heart CoA transferase and the expected mitochondrial targeting sequence enriched with Arg, Leu, and Ser in the N-terminal region. Thus, we termed this gene scot-t (testis-specific succinyl CoA:3-oxo acid CoA transferase). Northern blot analysis, in situ hybridization, and Western blot analysis demonstrated a unique expression pattern of the mRNA with rapid translation exclusively in late spermatids. The scot-t protein was detected first in elongated spermatids at step 8 or 9 as faint signals and gradually accumulated during spermiogenesis. It was also detected in the midpiece of spermatozoa by immunohistochemistry. The results suggest that the scot-t protein plays important roles in the energy metabolism of spermatozoa. (+info)

Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration. (6/146)

The tyrosine nitration of proteins has been observed in diverse inflammatory conditions and has been linked to the presence of reactive nitrogen species. From many in vitro experiments, it is apparent that tyrosine nitration may alter the function of proteins. A limited number of experiments under in vivo conditions also demonstrate that protein nitration is associated with altered cellular processes. To understand the association of protein nitration with the pathogenic mechanism of the disease, it is essential to identify specific protein targets of nitration with in vivo or intact tissue models. Using anti-nitrotyrosine antibodies, we demonstrated the accumulation of nitrotyrosine in a 52-kDa protein in rat kidney after lipopolysaccharide treatment. The 52-kDa protein was purified and identified with partial sequence as succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC ). Western blot analysis revealed that the nitration of this mitochondrial enzyme increased in the kidneys and hearts of lipopolysaccharide-treated rats, whereas its catalytic activity decreased. These data suggest that tyrosine nitration may be a mechanism for the inhibition of SCOT activity in inflammatory conditions. SCOT is a key enzyme for ketone body utilization. Thus, tyrosine nitration of the enzyme with sepsis or inflammation may explain the altered metabolism of ketone bodies present in these disorders. (+info)

Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. (7/146)

Anaerobic microbial toluene catabolism is initiated by addition of fumarate to the methyl group of toluene, yielding (R)-benzylsuccinate as first intermediate, which is further metabolized via beta-oxidation to benzoyl-coenzyme A (CoA) and succinyl-CoA. A specific succinyl-CoA:(R)-benzylsuccinate CoA-transferase activating (R)-benzylsuccinate to the CoA-thioester was purified and characterized from Thauera aromatica. The enzyme is fully reversible and forms exclusively the 2-(R)-benzylsuccinyl-CoA isomer. Only some close chemical analogs of the substrates are accepted by the enzyme: succinate was partially replaced by maleate or methylsuccinate, and (R)-benzylsuccinate was replaced by methylsuccinate, benzylmalonate, or phenylsuccinate. In contrast to all other known CoA-transferases, the enzyme consists of two subunits of similar amino acid sequences and similar sizes (44 and 45 kDa) in an alpha(2)beta(2) conformation. Identity of the subunits with the products of the previously identified toluene-induced bbsEF genes was confirmed by determination of the exact masses via electrospray-mass spectrometry. The deduced amino acid sequences resemble those of only two other characterized CoA-transferases, oxalyl-CoA:formate CoA-transferase and (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase, which represent a new family of CoA-transferases. As suggested by kinetic analysis, the reaction mechanism of enzymes of this family apparently involves formation of a ternary complex between the enzyme and the two substrates. (+info)

Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. (8/146)

High levels of reactive species of nitrogen and oxygen in diabetes may cause modifications of proteins. Recently, an increase in protein tyrosine nitration was found in several diabetic tissues. To understand whether protein tyrosine nitration is the cause or the result of the associated diabetic complications, it is essential to identify specific proteins vulnerable to nitration with in vivo models of diabetes. In the present study, we have demonstrated that succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC 2.8.3.5) is susceptible to tyrosine nitration in hearts from streptozotocin-treated rats. After 4 and 8 wk of streptozotocin administration and diabetes progression, SCOT from rat hearts had a 24% and 39% decrease in catalytic activity, respectively. The decrease in SCOT catalytic activity is accompanied by an accumulation of nitrotyrosine in SCOT protein. SCOT is a mitochondrial matrix protein responsible for ketone body utilization. Ketone bodies provide an alternative source of energy during periods of glucose deficiency. Because diabetes results in profound derangements in myocardial substrate utilization, we suggest that SCOT tyrosine nitration is a contributing factor to this impairment in the diabetic heart. (+info)

"Transcriptional and functional analysis of oxalyl-coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes from ... Oxalate-CoA ligase Formyl-CoA transferase Oxalate CoA-transferase Baetz AL, Allison MJ (July 1990). "Purification and ... No FAD binding is observed in oxalyl-CoA decarboxylase, but an excess of coenzyme A in the crystal structure has led to the ... characterization of formyl-coenzyme A transferase from Oxalobacter formigenes". Journal of Bacteriology. 172 (7): 3537-40. doi: ...

https://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase

This enzyme is also called hydroxycinnamoyl coenzyme A-quinate transferase. This enzyme participates in phenylpropanoid ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... The systematic name of this enzyme class is feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase. ... "Purification and characterization of hydroxycinnamoyl D-glucose Quinate hydroxycinnamoyl transferase in the root of sweet ...

https://en.wikipedia.org/wiki/Quinate_O-hydroxycinnamoyltransferase

2007). "A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency". Am. J. Hum. ... "Entrez Gene: COQ2 coenzyme Q2 homolog, prenyltransferase (yeast)". Human COQ2 genome location and COQ2 gene details page in the ... 2006). "Coenzyme Q and the regulation of intracellular steady-state levels of superoxide in HL-60 cells". BioFactors. 25 (1-4 ... 2005). "Coenzyme Q2 induced p53-dependent apoptosis". Biochim. Biophys. Acta. 1724 (1-2): 49-58. doi:10.1016/j.bbagen.2005.04. ...

https://en.wikipedia.org/wiki/COQ2

Other names in common use include isobutyryl coenzyme A mutase, and butyryl-CoA:isobutyryl-CoA mutase. It has 2 cofactors: ... This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The ... Willenbrock F, Robinson JA (1988). "The enzymic interconversion of isobutyryl and N-butyrylcarba(dethia)-coenzyme-A - a ... coenzyme-B12-dependent carbon skeleton rearrangement". Angew. Chem. Int. Ed. Engl. 27 (8): 1089-1091. doi:10.1002/anie. ...

https://en.wikipedia.org/wiki/Isobutyryl-CoA_mutase

The systematic name of this enzyme class is sinapoyl-CoA:2-hydroxymalonate O-(hydroxycinnamoyl)transferase. Other names in ... Strack D, Ruhoff R, Grawe W (1986). "Hydroxycinnamoyl-Coenzyme-A-tartronate hydroxycinnamoyltransferase in protein preparations ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... common use include tartronate sinapoyltransferase, and hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase. ...

https://en.wikipedia.org/wiki/Tartronate_O-hydroxycinnamoyltransferase

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Other names in common use include acylglycerol palmitoyltransferase, monoglyceride acyltransferase, acyl coenzyme A- ...

https://en.wikipedia.org/wiki/2-acylglycerol_O-acyltransferase

Tobin MB, Fleming MD, Skatrud PL, Miller JR (1990). "Molecular characterization of the acyl-coenzyme A:isopenicillin N ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Other names in common use include acyl-coenzyme A:isopenicillin N acyltransferase, and isopenicillin N:acyl-CoA: ... β-heterodimeric acyl-coenzyme A: isopenicillin N-acyltransferase of Penicillium chrysogenum". FEBS Letters. 319 (1-2): 166-170 ...

https://en.wikipedia.org/wiki/Isopenicillin_N_N-acyltransferase

KENNEDY EP, WEISS SB (1956). "The function of cytidine coenzymes in the biosynthesis of phospholipides". J. Biol. Chem. 222: ... This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. ... and phosphorylethanolamine-glyceride transferase. This enzyme participates in 3 metabolic pathways: aminophosphonate metabolism ...

https://en.wikipedia.org/wiki/Diacylglycerol_ethanolaminephosphotransferase

... coenzyme M-epoxyalkane ligase, epoxyalkyl:CoM transferase, epoxypropane:coenzyme M transferase, epoxypropyl:CoM transferase, ... coenzyme M transferase, epoxyalkane:CoM transferase, epoxyalkane:2-mercaptoethanesulfonate transferase, ... Coleman NV, Spain JC (September 2003). "Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation ... Allen JR, Clark DD, Krum JG, Ensign SA (July 1999). "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial ...

https://en.wikipedia.org/wiki/2-hydroxypropyl-CoM_lyase

Saylor MH, Mansell RL (1977). "Hydroxycinnamoyl: coenzyme A transferase involved in the biosynthesis of kaempferol-3-(p- ... This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than ...

https://en.wikipedia.org/wiki/Flavonol-3-O-triglucoside_O-coumaroyltransferase

... substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase". ... Studies have shown that homocysteine reacts with SDH's PLP coenzyme to create a complex. This complex is devoid of coenzyme ... Two monomers(left and right) are shown and the coenzyme PLP is placed in the crevice between the two domains. Two Dimers: Two ... The main role of SDH is to lower the activation energy of this reaction by binding the coenzyme and substrate in a particular ...

https://en.wikipedia.org/wiki/Serine_dehydratase

HOAGLAND MB, NOVELLI GD (1954). "Biosynthesis of coenzyme A from phospho-pantetheine and of pantetheine from pantothenate". J. ... This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups ( ... Martin DP, Drueckhammer DG (1993). "Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ... dephospho-coenzyme A pyrophosphorylase, and 3'-dephospho-CoA pyrophosphorylase. This enzyme participates in pantothenate and ...

https://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase

Other names in common use include acetyl coenzyme A:taxa-4(20),11(12)-dien-5alpha-ol O-acetyl, and transferase. Walker K, ... "Partial purification and characterization of acetyl coenzyme A: taxa-4(20),11(12)-dien-5alpha-ol O-acetyl transferase that ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

https://en.wikipedia.org/wiki/Taxadien-5alpha-ol_O-acetyltransferase

Strain B13: Purification and Characterization of 3-Oxoadipate:Succinyl-Coenzyme A (CoA) Transferase and 3-Oxoadipyl-CoA ... Strain B13: Cloning, Characterization, and Analysis of Sequences Encoding 3-Oxoadipate:Succinyl-Coenzyme A (CoA) Transferase ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

https://en.wikipedia.org/wiki/3-oxoadipyl-CoA_thiolase

KENNEDY EP, WEISS SB (1956). "The function of cytidine coenzymes in the biosynthesis of phospholipides". J. Biol. Chem. 222 (1 ... This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups ( ... Other names in common use include phosphorylethanolamine transferase, ET, CTP-phosphoethanolamine cytidylyltransferase, ...

https://en.wikipedia.org/wiki/Ethanolamine-phosphate_cytidylyltransferase

CPT-I inhibitors: Etomoxir, Oxfenicine, Perhexiline CPT-I (carnitine palmitoyl transferase) converts fatty acyl-CoA to fatty ... Carnitine biosynthesis inhibitor: Mildronate 3-KAT inhibitors: Trimetazidine 3-KAT (3-ketoacyl-coenzyme A thiolase) inhibitors ...

https://en.wikipedia.org/wiki/Fatty_acid_oxidation_inhibitors

Other names in common use include caffeoyl coenzyme A methyltransferase, caffeoyl-CoA 3-O-methyltransferase, and trans-caffeoyl ... This enzyme is classified to the family of transferases, specifically those transferring one-carbon group methyltransferases. ...

https://en.wikipedia.org/wiki/Caffeoyl-CoA_O-methyltransferase

coenzyme-A comes in and undergoes hydrogen-atom transfer with the Cys419 radical to generate a coenzyme-A radical. The coenzyme ... The reaction occurs as follows: This enzyme belongs to the family of transferases, specifically those acyltransferases ... Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl- ...

https://en.wikipedia.org/wiki/Formate_C-acetyltransferase

"Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ... "Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A ...

https://en.wikipedia.org/wiki/Biotin-independent_malonate_decarboxylase

Methyl- THMPT is the methyl donor to coenzyme M, a conversion mediated by methyl- THMPT:coenzyme M methyl-transferase. THMPT is ... Tetrahydromethanopterin (THMPT, H 4MPT) is a coenzyme in methanogenesis. It is the carrier of the C1 group as it is reduced to ... Methylene- MPT is subsequently converted, using coenzyme F420 as the electron source, to methyl- THMPT, catalyzed by F420- ... tetrahydromethanopterin formyltransferase in complex with its coenzymes". J. Mol. Biol. 357 (3): 870-9. doi:10.1016/j.jmb. ...

https://en.wikipedia.org/wiki/Tetrahydromethanopterin

Somack R, Costilow RN (1973). "Purification and properties of a pyridoxal phosphate and coenzyme B 12 dependent D- -ornithine 5 ... This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The ... It has 3 cofactors: pyridoxal phosphate, Cobamide coenzyme, and Dithiothreitol. ...

https://en.wikipedia.org/wiki/D-ornithine_4,5-aminomutase

DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL CARRIER PROTEIN AND COENZYME A ... transferase activity. • enoyl-[acyl-carrier-protein reductase (NADPH, A-specific) activity]. • 3-hydroxypalmitoyl-[acyl-carrier ...

https://en.wikipedia.org/wiki/Fatty_acid_synthase

Formyl-CoA transferase （EC 2.8.3.16）mediates the exchange of oxalyl and formyl groups on coenzyme A, interconverting formyl-CoA ... Enzymes in this class include oxalate oxidase, oxalate decarboxylase, oxalyl-CoA decarboxylase, and formyl-CoA transferase. ...

https://en.wikipedia.org/wiki/Oxalate_degrading_enzyme

... acetoacetate CoA-transferase, a novel prokaryotic member of the CoA-transferase family". The Journal of Biological Chemistry. ... Here they can be oxidized and combined with coenzyme A to form CO2, acetyl-CoA, and NADH, as in the normal cycle. However, it ... Mullins EA, Francois JA, Kappock TJ (July 2008). "A specialized citric acid cycle requiring succinyl-coenzyme A (CoA):acetate ... FADH2, therefore, facilitates transfer of electrons to coenzyme Q, which is the final electron acceptor of the reaction ...

https://en.wikipedia.org/wiki/Citric_acid_cycle

Hydroxycinnamoyl transferase (HCT) then converts p-coumaroyl CoA to 4-coumaroyl shikimate/quinate. This subsequently undergoes ... Then, in the proposed ferulate pathway, 4-hydroxycinnamoyl-CoA ligase (4CL) attaches p-coumaric acid to coenzyme A (CoA) to ...

https://en.wikipedia.org/wiki/Vanillin

... and lecithin retinol acyl transferase. Higa HH, Varki A (1988). "Acetyl-coenzyme A:polysialic acid O-acetyltransferase from K1- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ...

https://en.wikipedia.org/wiki/Polysialic-acid_O-acetyltransferase

ChAT catalyzes the transfer of an acetyl group from the coenzyme acetyl-CoA to choline, yielding acetylcholine (ACh). ChAT is ... Nachmanson & Machado, 1943 The acetyl transferase mode of action was unknown at the time of this discovery, however Nachmansohn ... Nachmansohn D, Berman M (1946). "Studies on choline acetylase; on the preparation of the coenzyme and its effect on the enzyme ... Jones DH, Nelson WL (1968). "A method for isolation of coenzyme A products". Anal. Biochem. 26 (3): 350-7. doi:10.1016/0003- ...

https://en.wikipedia.org/wiki/Choline_acetyltransferase

Other names in common use include flavonol 3-O-glucoside malonyltransferase, MAT-3, and malonyl-coenzyme A:flavonol-3-O- ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Matern U, Feser C, Hammer D (1983). "Further characterization and regulation of malonyl-coenzyme A: flavonoid glucoside ...

https://en.wikipedia.org/wiki/Flavonol-3-O-beta-glucoside_O-malonyltransferase

Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases". J. Biol. ... This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl ... Other names in common use include acetyl coenzyme A-acyl-carrier-protein transacylase, Acetyl CoA:ACP transacylase, [acyl- ...

https://en.wikipedia.org/wiki/(acyl-carrier-protein)_S-acetyltransferase

"Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ... dephospho-CoA-transferase. This enzyme catalyses the following chemical reaction 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + ... dephospho-CoA transferase, MdcG, 2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-malonate-decarboxylase adenylyltransferase, holo ... "Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase". ...

https://en.wikipedia.org/wiki/Malonate_decarboxylase_holo-(acyl-carrier_protein)_synthase

Dempski RE, Imperiali B (December 2002). "Oligosaccharyl transferase: gatekeeper to the secretory pathway". Curr Opin Chem Biol ... oligosaccharyl transferase complex) the newly synthesized protein is transported across the membrane (gray) into the interior ... "Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon". Nat. Commun. (5): 3072. ... "STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo". EMBO J. 14 (20): 4949-60. ...

https://en.wikipedia.org/wiki/Oligosaccharyltransferase

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The ...

https://en.wikipedia.org/wiki/Beta-alanine—pyruvate_transaminase

It is structurally similar to the coenzyme, folate, which binds to the enzyme dihydrofolate reductase.[3] This enzyme is part ... Transferase (EC 2). *2.1 COMT. *Thymidylate synthase. *2.4 PARP. *2.5 Dihydropteroate synthetase ...

https://en.wikipedia.org/wiki/Competitive_inhibition

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/2-alkenal_reductase

Transferases: acyltransferases (EC 2.3). 2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A ... "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ... transferase activity. • transferase activity, transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase ... transferase activity, transferring acyl groups. • 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C- ...

https://en.wikipedia.org/wiki/HADHB

In addition, the enzyme transferase shifts a block of 3 glucosyl residues from the outer branch to the other end, and then a α1 ...

https://en.wikipedia.org/wiki/Glycogen_phosphorylase

There are three well-known and -studied classes of SOD metallic coenzymes that exist in plants. First, Fe SODs consist of two ... EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Orgotein

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/L-xylulose_reductase

White HB (Mar 1976). "Coenzymes as fossils of an earlier metabolic state". Journal of Molecular Evolution. 7 (2): 101-4. ... Noller HF, Hoffarth V, Zimniak L (Jun 1992). "Unusual resistance of peptidyl transferase to protein extraction procedures". ... Ribonucleotide moieties in many coenzymes, such as Acetyl-CoA, NADH, FADH and F420, may be surviving remnants of covalently ... contains 23s rRNA which act as a peptide bond forming enzyme called peptidal transferase and helps in protein synthesis. Many ...

https://en.wikipedia.org/wiki/RNA_world

The transferase UDP-glucuronate pyrophosphorylase removes a UMP and glucuronokinase, with the cofactor ADP, removes the final ...

https://en.wikipedia.org/wiki/L-ascorbic_acid

transferase activity. • nucleotide binding. • protein kinase activity. • kinase activity. • protein serine/threonine kinase ...

https://en.wikipedia.org/wiki/CDK4

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Beta-glucosidase

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Homoisocitrate_dehydrogenase

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/AKR1B1

Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Phosphogluconate_dehydratase

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Factor_X

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/GTP_cyclohydrolase_II

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Succinyl-diaminopimelate_desuccinylase

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/GAD_antibodies

Cofactors, or coenzymes, are helper molecules which are needed to make an enzyme work. They are not proteins, and may be ... Transferases: move functional group from one molecule to another. *Hydrolases: add -OH (hydroxyl) group ...

https://simple.wikipedia.org/wiki/Enzyme

Ubiquinol (coenzyme Q) Lipid 5[84] 200 (human)[85] Uric acid[edit]. Uric acid is by far the highest concentration antioxidant ... Hayes JD, Flanagan JU, Jowsey IR (2005). "Glutathione transferases". Annual Review of Pharmacology and Toxicology. 45: 51-88. ... "Serum coenzyme Q10 concentrations in healthy men supplemented with 30 mg or 100 mg coenzyme Q10 for two months in a randomised ... Turunen M, Olsson J, Dallner G (January 2004). "Metabolism and function of coenzyme Q". Biochimica et Biophysica Acta. 1660 (1- ...

https://en.wikipedia.org/wiki/Free_radical_scavenger

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Complement_component_1s

transferase activity. • nucleotide binding. • protein kinase activator activity. • 1-phosphatidylinositol-4-phosphate 3-kinase ...

https://en.wikipedia.org/wiki/PIK3CA

The thiol from coenzyme A serves as a good leaving group when attacked by a general base to give N-acetylserotonin.[58] ... It has been proposed that histidine residue His122 of serotonin N-acetyl transferase is the catalytic residue that deprotonates ...

https://en.m.wikipedia.org/wiki/Melatonin

Transferases: acyltransferases (EC 2.3). 2.3.1: other than amino-acyl groups. *acetyltransferases: Acetyl-Coenzyme A ... Crystal structure of Tetrahymena Gcn5 with bound coenzyme A and histone H3 peptide (PDB 1QSN). The central core (green), ... flanking N- and C-terminal segments (blue), coenzyme A (orange), and histone peptide (red) are shown. ... "Lessons from genome-wide studies: an integrated definition of the coactivator function of histone acetyl transferases" ...

https://en.wikipedia.org/wiki/Histone_acetyltransferase

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Aspartate_protease

LDH in humans uses His(193) as the proton acceptor, and works in unison with the coenzyme (Arg99 and Asn138), and substrate ( ... EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Lactate_dehydrogenase

DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase. RNA nucleotidyltransferase. RNA polymerase/DNA-directed ...

https://en.wikipedia.org/wiki/Class_II_PI_3-kinases

EC2 Transferases (list). *EC3 Hydrolases (list). *EC4 Lyases (list). *EC5 Isomerases (list) ...

https://en.wikipedia.org/wiki/Homotropic_allosteric_interaction

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

http://www.ebi.ac.uk/interpro/protein/A6QHN4

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

http://www.rcsb.org/pdb/protein/Q9W058

Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial. A, D [auth B], C, B [auth D]. 481. Sus scrofa. Mutation(s): 0 ... The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase.. Coker, S.F., Lloyd, A.J., Mitchell, ... Dynamic domains of Succinyl-CoA:3-ketoacid-coenzyme A transferase from pig heart.. *DOI: 10.2210/pdb3K6M/pdb ... The enzyme succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) participates in the metabolism of ketone bodies in extrahepatic ...

https://www.rcsb.org/structure/3k6m

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaUniRule annotation. Automatic assertion according to rulesi ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha. Neisseria gonorrhoeae NG-k51.05 ...

https://www.uniprot.org/uniprot/A0A5K1QNE8

Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (accD), Acetyl-coenzyme A carboxylase carboxyl transferase ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit alphaUniRule annotation. ,p>Information which has been generated by ... tr,T5CLE2,T5CLE2_HELPX Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Helicobacter pylori FD506 GN=accA PE ...

http://www.uniprot.org/uniprot/T5CLE2

Burkholderia mallei Acetyl coenzyme A carboxylase carboxyl transferase subunit alpha accA - Gentaur.com - Product info ... Burkholderia mallei Acetyl coenzyme A carboxylase carboxyl transferase subunit alpha accA. Burkholderia mallei Acetyl coenzyme ... Gene targetBurkholderia mallei coenzyme carboxylase carboxyl transferase subunit alpha accA Baculovirus ... GEN1237410.E.coli , Burkholderia mallei Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) -E. coli size: ...

https://gentaur.com/868636459/burkholderia-mallei-acetyl-coenzyme-a/mbs?p=1023160866

Burkholderia phymatum Acetyl coenzyme A carboxylase carboxyl transferase subunit - Gentaur.com - Product info ... Burkholderia phymatum Acetyl coenzyme A carboxylase carboxyl transferase subunit. Burkholderia phymatum Acetyl coenzyme A ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) Alternative name Burkholderia phymatum Acetyl-coenzyme ... Gene targetBurkholderia phymatum coenzyme carboxylase carboxyl transferase subunit alpha accA Mammalian ...

https://gentaur.com/1698932813/burkholderia-phymatum-acetyl-coenzyme-a/mbs?p=1023410537

... coenzyme A transferase (Clostridium kluyveri DSM 555). Find diseases associated with this biological target and compounds ...

https://pubchem.ncbi.nlm.nih.gov/protein/P38946

Recombinant Protein and Probable coenzyme A transferase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Probable coenzyme A transferase subunit alpha. Probable coenzyme A transferase subunit alpha ELISA Kit. Probable coenzyme A ... Probable coenzyme A transferase subunit beta. Probable coenzyme A transferase subunit beta ELISA Kit. Probable coenzyme A ... Probable coenzyme A transferase subunit beta Antibody. Also known as Probable coenzyme A transferase subunit beta (Probable CoA ...

https://www.mybiosource.com/protein_family.php?root=probable-coenzyme-a-transferase

Monkey 3-Oxoacid Coenzyme A Transferase 1 ELISA Kit-AIC49324.1 (MBS074178) product datasheet at MyBioSource, ELISA Kits ... OXCT1 elisa kit :: Monkey 3-Oxoacid Coenzyme A Transferase 1 ELISA Kit. ... Kit for analyzing the presence of the 3-Oxoacid Coenzyme A Transferase 1 (OXCT1) ELISA Kit target analytes in biological ... 3-Oxoacid Coenzyme A Transferase 1 (OXCT1), ELISA Kit. Also Known As Monkey 3-Oxoacid Coenzyme A Transferase 1 ELISA Kit. ...

https://www.mybiosource.com/prods/ELISA-Kit/Monkey/3-Oxoacid-Coenzyme-A-Transferase-1/OXCT1/datasheet.php?products_id=74178

What is Acyl-Coenzyme A:Cholesterol O-Transferase? Meaning of Acyl-Coenzyme A:Cholesterol O-Transferase medical term. What does ... Cholesterol O-Transferase in the Medical Dictionary? Acyl-Coenzyme A:Cholesterol O-Transferase explanation free. ... Looking for online definition of Acyl-Coenzyme A: ... Acyl-Coenzyme A:Cholesterol O-Transferase. *acyl-malonyl-ACP ... Acyl-Coenzyme A:Cholesterol O-Transferase , definition of Acyl-Coenzyme A:Cholesterol O-Transferase by Medical dictionary https ...

https://medical-dictionary.thefreedictionary.com/Acyl-Coenzyme+A%3ACholesterol+O-Transferase

BLAST of Succinyl-CoA:3-ketoacid-coenzyme A transferase vs. TrEMBL. *BLAST of Succinyl-CoA:3-ketoacid-coenzyme A transferase vs ... Coenzyme A transferase family I. PANTHER. PTHR13707. KETOACID-COENZYME A TRANSFERASE. coord: 2..125. ... 3-ketoacid-coenzyme A transferase OS=... [more]. A0A1U7S2D6. 8.280e-49. 64.80. succinyl-CoA:3-ketoacid coenzyme A transferase 1 ... 3-ketoacid coenzyme A transferase 1, ... [more]. oxct1a. 3.357e-44. 61.60. succinyl-CoA:3-ketoacid coenzyme A transferase 1 ...

https://planosphere.stowers.org/feature/Schmitea/mediterranea-sexual/transcript/SMED30015906

HCA RNA Cell Line for Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial. ... Compartment GO Terms for Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial. ...

https://pharos.nih.gov/idg/targets/Q9BYC2

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGA ... Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin ...

http://ecmdb.ca/proteins/P0ABD5

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta MSWIERIKSNITPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMTARNR ... Li, S. J., Cronan, J. E. Jr (1993). "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes ... open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase." J Bacteriol 174:5755-5757. Pubmed: ...

http://ecmdb.ca/proteins/P0A9Q5

Yeast 01022793307 at Gentaur Vibrio cholerae serotype O1 coenzyme A carboxylase carboxyl transferase subunit alpha (accA) Yeast ... Order Vibrio cholerae serotype O1 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha accA - ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha(accA) is a recombinant protein expressed in Yeast . The ... N terminal acetylation or CH3CO as epigenetic regulation of Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha( ...

https://polabo.com/shop/11-mbs-recombinant/27406-acetyl-coenzyme-a-carboxylase-carboxyl-transferase-subunit-alpha-acca

Salmonella paratyphi C Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) datasheet and description hight ... Salmonella paratyphi C Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA). Contact us. ... Salmonella paratyphi C coenzyme A carboxylase carboxyl transferase subunit alpha (accA). Short name: Salmonella paratyphi C - ... Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, acetyl-CoA carboxylase carboxyltransferase subunit alpha. ...

https://gentaursearch.com/product/salmonella/803543/salmonella-paratyphi-c-acetyl-coenzyme-a-carboxylase-carboxyl-transferase-subunit-alpha-acca.html

Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A ( ... "Group" would be the functional group transferred as a result of transferase activity. The donor is often a coenzyme. Some of ... Transferase deficiencies are at the root of many common illnesses. The most common result of a transferase deficiency is a ... Terminal transferases are transferases that can be used to label DNA or to produce plasmid vectors. It accomplishes both of ...

https://en.wikipedia.org/wiki/Transferase

3-oxoacid CoA-transferase (SCOT) deficiency is an inborn error of ketone body utilization, characterized by intermittent ... Coenzyme A-Transferases / deficiency* * Coenzyme A-Transferases / genetics* * Glucose / administration & dosage * Glucose / ... Neonatal hypoglycaemia in severe succinyl-CoA: 3-oxoacid CoA-transferase deficiency J Inherit Metab Dis. 2001 Oct;24(5):587-95. ... Succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency is an inborn error of ketone body utilization, characterized by ...

https://pubmed.ncbi.nlm.nih.gov/11757586/?dopt=Abstract

And then there were acyl coenzyme A:cholesterol acyl transferase inhibitors. Meuwese, Marijn C; Franssen, Remco; Stroes, Erik ...

https://journals.lww.com/co-lipidology/toc/2006/08000

Other names in common use include 3-oxoacid coenzyme A-transferase, 3-ketoacid CoA-transferase, 3-ketoacid coenzyme A ... succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA transferase. This enzyme participates in 3 metabolic ... transferase, 3-oxo-CoA transferase, 3-oxoacid CoA dehydrogenase, acetoacetate succinyl-CoA transferase, acetoacetyl coenzyme A- ... Preparation and properties of coenzyme A transferase". J. Biol. Chem. 221 (1): 15-31. PMID 13345795. Biology portal v t e. ...

https://en.wikipedia.org/wiki/3-oxoacid_CoA-transferase

... succinyl-CoA acetoacetyl-CoA transferase; Co-A, co-enzyme A; α-KG, α-ketoglutarate; (m), mitochondrial; (c) cytosolic; TCA, ... tricarboxylic acid; AAT, aspartate amino transferase; GDH, glutamate dehydrogenase; BBB, blood-brain barrier. ...

https://www.ncbi.nlm.nih.gov/pubmed/27142056

AcCoA: acetyl-coenzyme A; ACh: acetylcholine; AChE: acetylcholinesterase; ChAT: acetylcholine transferase; CYP450: Cytochrome ...

https://www.hindawi.com/journals/jir/2015/213836/

KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; KW Nucleotide-binding; Transferase. FT CHAIN 1..206 FT /note=" ... DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1. DR ... coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 5/5. {ECO:0000255,HAMAP-Rule:MF_00376}. CC -!- SUBCELLULAR ... dephosphocoenzyme A to form coenzyme A. {ECO:0000255,HAMAP- CC Rule:MF_00376}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3- ...

http://pbil.univ-lyon1.fr/cgi-bin/acnuc-search-ac?query=AAZ86906&db=SWISSPROT&ident=ACNUC7421

View mouse Acbd3 Chr1:180726043-180754204 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression

http://www.informatics.jax.org/marker/MGI:2181074

... carnitine palmitoyl transferase 1a; Acox1: acyl-coenzyme A oxidase 1); (C) Expressions of lipogenesis-related genes in liver ( ... carnitine palmitoyl transferase 1a; Acox1: acyl-coenzyme A oxidase 1); (C) Expressions of lipogenesis-related genes in liver ( ... carnitine palmitoyl transferase 1a (Cpt1a), and acyl-coenzyme A oxidase 1 (Acox1), were significantly elevated in mice fed with ...

https://www.mdpi.com/1420-3049/22/5/699/htm

Ac-CoA, acetyl coenzyme A; F-6-P, fructose 6-phosphate; G-3-P, glucose 3-phosphate; OGT, O-GlcNAc transferase; TCA, ...

https://www.jci.org/articles/view/72271

T1 - Acetate utilization and butyryl coenzyme A (CoA). T2 - acetate-CoA transferase in butyrate-producing bacteria from the ... Acetate utilization and butyryl coenzyme A (CoA): acetate-CoA transferase in butyrate-producing bacteria from the human large ... Acetate utilization and butyryl coenzyme A (CoA): acetate-CoA transferase in butyrate-producing bacteria from the human large ... Acetate utilization and butyryl coenzyme A (CoA) : acetate-CoA transferase in butyrate-producing bacteria from the human large ...

https://abdn.pure.elsevier.com/en/publications/acetate-utilization-and-butyryl-coenzyme-a-coa-acetate-coa-transf

Succinyl-CoA:3-ketoacid-coenzyme A transferase. Increase. Temporal cortex. 2DE-MS. 156. ... 3-ketoacid-coenzyme A transferase 1, mitochondrial glutamate carrier 1. Increase. Frontal cortex. LC-MS (iTRAQ). 177. ...

https://www.medscape.com/viewarticle/726511

acyl-coenzyme A oxidase 58. -. Vitis coignetiae Pulliat leaves (yama-budo). Rats on HFD choline deficient diet. liver enzymes ... chol: cholesterol; FFAs: free fatty acids; CPT-1: carnitine-palmitoyl-transferase-1; HMG-CoA red: 3-hydroxymethyl-3-glutaryl- ... AMPK: adenosine monophosphate protein kinase; Srebp1c: sterol regulated element binding protein 1c; ACC: acetyl-coenzyme A ... acetyl-coenzyme A carboxylase; ROS: reactive oxygen species; JNK: c-Jun N-terminal kinase; FOXO1: forkhead box O1.. ...

https://www.hindawi.com/journals/omcl/2013/145421/

Transcriptional and functional analysis of oxalyl-coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes from Lactobacillus acidophilus . (springer.com)
Lactose-inducible expression of the four heterologous genes necessary to convert acetyl coenzyme A (acetyl-CoA) to acetone diverted ca. 60% of carbon flow to acetone production during growth on fructose, and 25% of carbon flow went to acetone when carbon monoxide was the electron donor. (asm.org)
Genes for the putative A and B subunits of H.pylori CoA-transferase were introduced into the bacterial expressionvector pKK223-3 and expressed in Escherichia coli JM105 cells. (embl.de)
3050, or ninety seven percent of the [http://en.wikipedia.org/wiki/Genes genes] all code for proteins, meaning that a large portion of ''Acetobacter aceti'' is to produce protein. (kenyon.edu)
In this study we describe a gene-targeted approach for 454 pyrotag sequencing andquantitative polymerase chain reaction for the final genes in the two primarybacterial butyrate synthesis pathways, butyryl-CoA:acetate CoA-transferase( but ) and butyrate kinase ( buk ). (biomedcentral.com)

The enzyme succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) participates in the metabolism of ketone bodies in extrahepatic tissues. (rcsb.org)
MBS074178 is a ready-to-use microwell, strip plate ELISA (enzyme-linked immunosorbent assay) Kit for analyzing the presence of the 3-Oxoacid Coenzyme A Transferase 1 (OXCT1) ELISA Kit target analytes in biological samples. (mybiosource.com)
Mechanistically, an enzyme that catalyzed the following reaction would be a transferase: X g r o u p + Y → t r a n s f e r a s e X + Y g r o u p {\displaystyle Xgroup+Y{\xrightarrow[{transferase}]{}}X+Ygroup} In the above reaction, X would be the donor, and Y would be the acceptor. (wikipedia.org)
In 1953, the enzyme UDP-glucose pyrophosphorylase was shown to be a transferase, when it was found that it could reversibly produce UTP and G1P from UDP-glucose and an organic pyrophosphate. (wikipedia.org)
In enzymology, a 3-oxoacid CoA-transferase (EC 2.8.3.5) is an enzyme that catalyzes the chemical reaction succinyl-CoA + a 3-oxo acid ⇌ {\displaystyle \rightleftharpoons } succinate + a 3-oxoacyl-CoA Thus, the two substrates of this enzyme are succinyl-CoA and 3-oxo acid, whereas its two products are succinate and 3-oxoacyl-CoA. (wikipedia.org)
This enzyme belongs to the family of transferases, specifically the CoA-transferases. (wikipedia.org)
The systematic name of this enzyme class is succinyl-CoA:3-oxo-acid CoA-transferase. (wikipedia.org)
It is concluded that succinate dehydrogenase activity in the pineal gland of the rat is regulated by changing the concentration of the active enzyme itself as well as the level of the endogenous coenzyme Q. Whether this is caused by a circadian rhythm in the synthesis or in the catabolism of the enzyme and the coenzyme was not revealed by the present study. (springer.com)
The researchers identified an enzyme (coniferyl ferulate feruloyl-CoA monolignol transferase) in other plants that contain more digestible lignin monomers, then expressed it in poplar. (greencarcongress.com)
Amino acidsequence comparisons, combined with measurements of enzyme activitiesusing different CoA donors and acceptors, identified the H. pyloriCoA-transferase as a succinyl CoA:acetoacetate CoA-transferase. (embl.de)
Addition of BES to cell extracts resulted in an irreversible loss of epoxide carboxylase activity that was restored by addition of purified 2-ketopropyl-CoM carboxylase/oxidoreductase (2-KPCC), the terminal enzyme of epoxide carboxylation, but not by addition of epoxyalkane:CoM transferase or 2-hydroxypropyl-CoM dehydrogenase, the enzymes which catalyze the first two reactions of epoxide carboxylation. (asm.org)
Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate. (kegg.jp)

Enzymic synthesis and metabolism of malonyl coenzyme A and glutaryl coenzyme A". J. Biol. (wikipedia.org)
Three key enzymes of the Clostridium acetobutylicum ATCC 824 metabolism, namely thiolase, phosphotransbutyrylase (PTB), and CoA transferase, were purified to homogeneity. (rice.edu)
Acetobacter aceti'' is an obligatory aerobic bacterium that can fix nitrogen during its metabolic processes and is known for producing [http://en.wikipedia.org/wiki/Alcohol alcohol] as a byproduct of its metabolism. (kenyon.edu)
Acetyl coenzyme A (acetyl-CoA) produced during β-oxidation is transported via the cytosol into mitochondria for further metabolism. (apsnet.org)

strain L2-50 is a net producer of acetate and possessed detectable butyrate kinase, acetate kinase, and butyryl-CoA:acetate-CoA transferase activities. (elsevier.com)

Other names in common use include 3-oxoacid coenzyme A-transferase, 3-ketoacid CoA-transferase, 3-ketoacid coenzyme A transferase, 3-oxo-CoA transferase, 3-oxoacid CoA dehydrogenase, acetoacetate succinyl-CoA transferase, acetoacetyl coenzyme A-succinic thiophorase, succinyl coenzyme A-acetoacetyl coenzyme A-transferase, and succinyl-CoA transferase. (wikipedia.org)

Description N terminal acetylation or CH3CO as epigenetic regulation of Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) by NATs.The Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) is a α- or alpha protein sometimes glycoprotein present in blood. (gentaur.com)
Description N terminal acetylation or CH3CO as epigenetic regulation of Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) by NATs.The Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (accA) is a α- or alpha protein sometimes glycoprotein present in blood.For cells, cell lines and tissues in culture till half confluency. (gentaur.com)
Also known as Probable coenzyme A transferase subunit alpha (Probable CoA-transferase subunit alpha). (mybiosource.com)

Activation of acyl-coenzyme A:cholesterol acyl-transferase activity by cholesterol is not due to altered mRNA levels in HepG2 cells. (nii.ac.jp)

Succinyl-CoA: 3-oxoacid CoA-transferase (SCOT) deficiency is an inborn error of ketone body utilization, characterized by intermittent ketoacidotic crises and persistent ketosis. (nih.gov)
3-ketoacid CoA transferase ( SCOT ) deficiency causes episodic ketoacidotic crises and no apparent symptoms between them. (antikoerper-online.de)

Auf www.antikoerper-online.de finden Sie aktuell 57 3-Oxoacid CoA Transferase 1 (OXCT1) Antikörper von 16 unterschiedlichen Herstellern. (antikoerper-online.de)

Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters, the action of N-acetyltransferase, which is part of the pathway that metabolizes tryptophan, and the regulation of pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl CoA. (wikipedia.org)
Acetyl coenzyme A (acetyl-CoA), the central intermediate in the Wood-Ljungdahl pathway, can potentially serve as a precursor for the enzymatic production of a wide diversity of organic compounds ( 4 , 13 , 17 , 18 ). (asm.org)
For these strains, epoxyalkane:CoM transferase (EaCoMT) forms hydroxyethylthioether conjugates which are believed to undergo subsequent dehydrogenation and conversion to acetyl-CoA rather than carboxylation ( 15 ). (asm.org)
A peroxisomal-specific pathway for acetyl-CoA transport requiring peroxisomal carnitine acetyl transferase (CAT) activity has been identified in Magnaporthe grisea peroxisomes. (apsnet.org)

A transferase is any one of a class of enzymes that enact the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor). (wikipedia.org)
This same action by the transferase can be illustrated as follows: methylamine + L-glutamate ⇌ {\displaystyle \rightleftharpoons } NH3 + N-methyl-L-glutamate However, other accepted names are more frequently used for transferases, and are often formed as "acceptor grouptransferase" or "donor grouptransferase. (wikipedia.org)
For example, a DNA methyltransferase is a transferase that catalyzes the transfer of a methyl group to a DNA acceptor. (wikipedia.org)
3 -S bond into methane involves a ternary complex of methyl coenzyme M and coenzyme B fit into a channel terminated by the axial site on nickel of the cofactor F430. (wikipedia.org)
[7] These organisms may accomplish reverse methanogenesis using a nickel-containing protein similar to methyl-coenzyme M reductase used by methanogenic archaea. (wikipedia.org)
Molecular characterization and functional analysis of Glycine max sterol methyl transferase 2. (deepdyve.com)
With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90 , methanol---corrinoid protein Co-methyltransferase, and EC 2.1.1.246 , [methyl-Co(III) methanol-specific corrinoid protein]---coenzyme M methyltransferase). (kegg.jp)
The MtsA subunit of the methylthiol:coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer. (kegg.jp)

It catalyses the transfer of coenzyme A (CoA) from succinyl-CoA to acetoacetate with a classical ping-pong mechanism. (rcsb.org)
Cloning and characterization of Helicobacter pylori succinylCoA:acetoacetate CoA-transferase, a novel prokaryotic member of theCoA-transferase family. (embl.de)
The epoxypropane enantiomers are subsequently metabolized by a three-step linear pathway that uses four enzymes and the atypical cofactor coenzyme M (CoM) (2-mercaptoethanesulfonic acid) to catalyze the net carboxylation of epoxypropane to form the central metabolite acetoacetate, as shown in Fig. 1 ( 1 , 2 , 4 , 5 , 20 , 27 ). (asm.org)

Probably it is the beta subunit of a heterodimeric coenzyme A transferase. (cbd.int)

Metabolically-engineered cyanobacteria introduced with a heterologous Coenzyme A (CoA)-dependent pathway modified from Clostridium species can convert atmospheric CO 2 into 1-butanol. (springer.com)

A possible pathway for phaselic acid biosynthesis predicts a hydroxycinnamoyl transferase (HCT) capable of forming caffeoyl and/or p -coumaroyl esters with malate. (plantphysiol.org)
Together, these results indicate that HCT1 is involved in monolignol biosynthesis and HCT2 is a novel transferase likely involved in phaselic acid biosynthesis. (plantphysiol.org)
The sequence similarity of RhlA to transacylases, such as PhaG ( 26 ), which is involved in poly-β-hydroxyalkanoate (PHA) biosynthesis, led to the proposal that RhlA is a transacylase that catalyzes the transfer of β-hydroxydecanoyl moieties from acyl carrier protein (ACP) to coenzyme A (CoA) ( 8 ). (asm.org)

ATP:co(I)rrinoid adenosyltransferase (ACAT) enzymes convert vitamin B12 to coenzyme B12. (nih.gov)

The midway gene encodes a protein similar to mammalian acyl coenzyme A: diacylglycerol acyltransferase (DGAT), which converts diacylglycerol (DAG) into triacylglycerol (TAG). (genetics.org)

The symbionts appear to be auxotrophic for some vitamins, but have the potential to produce most amino acids as well as rare cofactors like coenzyme F 420 . (pnas.org)

and F. prausnitzii possessed butyryl coenzyme A (CoA):acetate-CoA transferase and acetate kinase activities, but butyrate kinase activity was not detectable either in growing or in stationary-phase cultures. (elsevier.com)

A relative lack of endogenous coenzyme Q, as well as a circadian rhythm of this coenzyme, highly influenced the activity of succinate dehydrogenase. (springer.com)

V. The oxidoreductases, the transferases and the hydrolases of the pineal gland. (springer.com)

Oxidoreductases and transferases account for about 50 percent of the approximately 1,000 enzymes recognized thus far. (britannica.com)

Another example of historical significance relating to transferase is the discovery of the mechanism of catecholamine breakdown by catechol-O-methyltransferase. (wikipedia.org)
For example, methylamine:L-glutamate N-methyltransferase would be the standard naming convention for the transferase methylamine-glutamate N-methyltransferase, where methylamine is the donor, L-glutamate is the acceptor, and methyltransferase is the EC category grouping. (wikipedia.org)

Transferases are involved in myriad reactions in the cell. (wikipedia.org)
The other four groups of reactions are the transferases -which catalyze reactions in which substances other than hydrogen are transferred-the lyases , the isomerases , and the ligases . (britannica.com)
They catalyse reversible transfer reactions of coenzyme A groups from CoA-thioesters to free acids. (embl.de)

Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes . (springer.com)

Poplar vascular tissue showing feruloyl-coenzyme A (CoA) monolignol transferase (FMT) expression. (greencarcongress.com)

OXCT2 (3-Oxoacid CoA-Transferase 2) is a Protein Coding gene. (genecards.org)

Systematic names of transferases are constructed in the form of "donor:acceptor grouptransferase. (wikipedia.org)

Group" would be the functional group transferred as a result of transferase activity. (wikipedia.org)
Earliest discoveries of transferase activity occurred in other classifications of enzymes, including Beta-galactosidase, protease, and acid/base phosphatase. (wikipedia.org)
GO annotations related to this gene include 3-oxoacid CoA-transferase activity and CoA-transferase activity . (genecards.org)
Activity assays of HCT1 and HCT2 proteins expressed in Escherichia coli indicate that HCT1 transfers caffeoyl or p -coumaroyl moieties from a coenzyme A-thiolester to shikimate but not malate, whereas HCT2 transfers caffeoyl or p -coumaroyl moieties from a coenzyme A-thiolester to malate but not shikimate. (plantphysiol.org)

A multisubunit form of acetyl coenzyme A (CoA) carboxylase (ACCase) from soybean ( Glycine max ) was characterized. (plantphysiol.org)

Thisactivity was consistently observed in different H. pylori strains.Antibodies raised against either recombinant A or B subunits recognizedtwo distinct subunits of Mr approximately 26,000 and 24, 000 that are bothnecessary for H. pylori CoA-transferase function. (embl.de)

These are organic compounds containing a 3-oxo acylated coenzyme A derivative. (hmdb.ca)

These NATs transfer the acetyl group from acetyl-coenzyme A to the amine group. (news-medical.net)
Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. (embl.de)

Acetobacter aceti'' is a non-pathogenic, [http://en.wikipedia.org/wiki/Gram_negative gram negative] prokaryote that converts ethanol to acetic acid with the presence of oxygen, making it an [http://en.wikipedia.org/wiki/Obligate_aerobe obligate aerobe]. (kenyon.edu)

Anatomy9

Organisms15

Diseases1

Chemicals and Drugs156

Analytical, Diagnostic and Therapeutic Techniques and Equipment25

Phenomena and Processes46

Disciplines and Occupations1

Information Science5

Health Care1

A functional 4-hydroxysalicylate/hydroxyquinol degradative pathway gene cluster is linked to the initial dibenzo-p-dioxin pathway genes in Sphingomonas sp. strain RW1. (1/146)

Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis. (2/146)

Regulation and adaptation of glucose metabolism of the parasitic protist Leishmania donovani at the enzyme and mRNA levels. (3/146)

Protection of mice against brucellosis by vaccination with Brucella melitensis WR201(16MDeltapurEK). (4/146)

Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase. (5/146)

Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration. (6/146)

Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. (7/146)

Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. (8/146)

Coenzyme A

Coenzymes

Transferases

Glutathione Transferase

Alkyl and Aryl Transferases

Coenzyme A-Transferases

Ubiquinone

Acetyl Coenzyme A

Coenzyme A Ligases

Transferases (Other Substituted Phosphate Groups)

DNA Nucleotidylexotransferase

Cobamides

Hydroxymethylglutaryl CoA Reductases

Molecular Sequence Data

Kinetics

Mesna

Acyltransferases

Substrate Specificity

NAD

Peptidyl Transferases

Amino Acid Sequence

N-Acetylglucosaminyltransferases

Pantothenic Acid

ADP Ribose Transferases

Farnesyltranstransferase

Escherichia coli

Mevalonic Acid

Liver

Pantetheine

Base Sequence

Euryarchaeota

Catalysis

Nucleotidyltransferases

Propanediol Dehydratase

Binding Sites

Protein Prenylation

Cloning, Molecular

Dinitrochlorobenzene

NADP

Hydroxymethylglutaryl-CoA Reductase Inhibitors

Methanosarcina barkeri

Galactosyltransferases

N-Acetylgalactosaminyltransferases

Palmitoyl Coenzyme A

Alcohol Oxidoreductases

Lovastatin

Acetate-CoA Ligase

Riboflavin

Methyltransferases

Isoenzymes

Malonyl Coenzyme A

Sequence Homology, Amino Acid

Oxidoreductases

gamma-Glutamyltransferase

Mutation

Methanobacterium

Bacterial Proteins

Glycosyltransferases

Polyisoprenyl Phosphates

Oxidation-Reduction

Acetyltransferases

DNA Nucleotidyltransferases

Sulfurtransferases

Recombinant Proteins

Models, Molecular

Hexosyltransferases

Pentosyltransferases

Protein Binding

Hydrogen-Ion Concentration

Acetates

Chromatography, High Pressure Liquid

UTP-Hexose-1-Phosphate Uridylyltransferase

Pyridoxal Phosphate

Molecular Weight

Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent

Methylmalonyl-CoA Mutase

Glutathione

Simvastatin

Genes, Bacterial

Acetylglucosamine