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EC 3.1
This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. EC 3.1: Acting on Ester Bonds EC 3.1.1: Carboxylic Ester Hydrolases * : carboxylesterase * : arylesterase * : triacylglycerol lipase * : phospholipase A2 * : lysophospholipase * : acetylesterase * : acetylcholinesterase * : cholinesterase * EC 3.1.1.9: deleted, a side reaction of cholinesterase * : tropinesterase * : pectinesterase * EC 3.1.1.12: deleted, identical with carboxylesterase * : sterol esterase * : chlorophyllase * : L-arabinonolactonase * EC 3.1.1.16: deleted, mixture of (muconolactone Δ-isomerase) and (3-oxoadipate enol-lactonase) * : gluconolactonase * EC 3.1.1.18: deleted, now included with gluconolactonase * ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme Commission Number
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. Furthermore, through convergent evolution, completely different protein folds can catalyze an identical reaction (these are sometimes called non-homologous isofunctional enzymes) and therefore would be assigned the same EC number. By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence. Format of number Every enzyme code consists of the letters "EC" followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme. Preliminary ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Uronolactonase
The enzyme uronolactonase (EC 3.1.1.19) catalyzes the reaction :D-glucurono-6,2-lactone + H2O \rightleftharpoons D-glucuronate This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... is D-glucurono-6,2-lactone lactonohydrolase. It is also called glucuronolactonase. It participates in ascorbate and aldarate metabolism. References * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
6-acetylglucose Deacetylase
The enzyme 6-acetylglucose deacetylase (EC 3.1.1.33) catalyzes the reaction :6-acetyl-D-glucose + H2O \rightleftharpoons D-glucose + acetate This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... of this enzyme class is 6-acetyl-D-glucose acetylhydrolase. This enzyme is also called 6-''O''-acetylglucose deacetylase. References * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phospholipase A1
Phospholipase A1 (EC 3.1.1.32; systematic name: phosphatidylcholine 1-acylhydrolase) encoded by the PLA1A gene is a phospholipase enzyme which removes the 1-acyl group: :phosphatidylcholine + H2O ⇌ 2-acylglycerophosphocholine + a carboxylate It is an enzyme that resides in a class of enzymes called phospholipase that hydrolyze phospholipids into fatty acids. There are four classes, separated according to the type of reaction they catalyze. In particular, phospholipase A1 (PLA1) specifically catalyzes the cleavage at the ''sn''-1 position of phospholipids, forming a fatty acid and a lysophospholipid. Function PLA1's are present in numerous species including humans, and have a variety of cellular functions that include regulation and facilitation of the production of lysophospholipid mediators, and acting as digestive enzymes. These enzymes are responsible for fast turnover rates of cellular phospholipids. In addition to this, the products of the reaction catalyzed by ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
6-phosphogluconolactonase
6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway: :6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate The tertiary structure of 6PGL employs an α/β hydrolase fold, with active site residues clustered on the loops of the α-helices. Based on the crystal structure of the enzyme, the mechanism is proposed to be dependent on proton transfer by a histidine residue in the active site. 6PGL selectively catalyzes the hydrolysis of δ-6-phosphogluconolactone, and has no activity on the γ isomer. Enzyme Mechanism 6PGL hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid has been proposed to proceed via proton transfer to the O5 ring oxygen atom, similar to xylose isomerase and ribose-5-phosphate isomerase. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
D-arabinonolactonase
The enzyme D-arabinonolactonase (EC 3.1.1.30) the reaction :D-arabinono-1,4-lactone + H2O \rightleftharpoons D-arabinonate This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... is D-arabinono-1,4-lactone lactonohydrolase. References * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aminoacyl-tRNA Hydrolase
The enzyme aminoacyl-tRNA hydrolase (EC 3.1.1.29) catalyzes the reaction :''N''-substituted aminoacyl-tRNA + H2O \rightleftharpoons ''N''-substituted amino acid + tRNA This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is aminoacyl-tRNA aminoacylhydrolase. Other names in common use include aminoacyl-transfer ribonucleate hydrolase, ''N''-substituted aminoacyl transfer RNA hydrolase, and peptidyl-tRNA hydrolase. Structural studies As of late 2007, 9 structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ... have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and . References * EC 3.1.1 Enzymes of known structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Acylcarnitine Hydrolase
The enzyme acylcarnitine hydrolase (EC 3.1.1.28) catalyzes the reaction :''O''-acylcarnitine + H2O \rightleftharpoons a fatty acid + L-carnitine This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... is ''O''-acylcarnitine acylhydrolase. Other names in common use include high activity acylcarnitine hydrolase, HACH, carnitine ester hydrolase, palmitoylcarnitine hydrolase, palmitoyl-L-carnitine hydrolase, long-chain acyl-L-carnitine hydrolase, and palmitoyl carnitine hydrolase. References * * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
4-pyridoxolactonase
The enzyme 4-pyridoxolactonase (EC 3.1.1.27) catalyzes the reaction :4-pyridoxolactone + H2O \rightleftharpoons 4-pyridoxate This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... is 4-pyridoxolactone lactonohydrolase. It participates in vitamin B6 metabolism. References * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Galactolipase
The enzyme galactolipase (EC 3.1.1.26) catalyzes the reaction :1,2-diacyl-3-β-D-galactosyl-''sn''-glycerol + 2 H2O \rightleftharpoons 3-β-D-galactosyl-''sn''-glycerol + 2 carboxylates This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... of this enzyme class is 1,2-diacyl-3-β-D-galactosyl-''sn''-glycerol acylhydrolase. Other names in common use include galactolipid lipase, polygalactolipase, and galactolipid acylhydrolase. This enzyme participates in glycerolipid metabolism. References * * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
1,4-lactonase
The enzyme 1,4-lactonase (EC 3.1.1.25) catalyzes the generic reaction :a 1,4-lactone + H2O \rightleftharpoons a 4-hydroxyacid This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 1,4-lactone hydroxyacylhydrolase. It is also called γ-lactonase. It participates in galactose metabolism and ascorbate and aldarate metabolism. It employs one cofactor, Ca2+. Structural studies As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes , , and . Applications In a study by Chen et al. a 1,4-lactonase was expressed in ''E. coli'' and used as a highly efficient biocatalyst for asymmetric synthesis Enantioselective synthesis, also called asymmetric synthesis, is a form of chemical synthesis. It is defined by IUPAC as "a chemical reaction (or reaction sequence) in which one or more new elements of chirality are formed in a substrate molecul ... of chiral compoun ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
3-oxoadipate Enol-lactonase
The enzyme 3-oxoadipate enol-lactonase (EC 3.1.1.24) catalyzes the reaction :3-oxoadipate enol-lactone + H2O \rightleftharpoons 3-oxoadipate This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... is 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase. Other names in common use include carboxymethylbutenolide lactonase, β-ketoadipic enol-lactone hydrolase, 3-ketoadipate enol-lactonase, 3-oxoadipic enol-lactone hydrolase, and β-ketoadipate enol-lactone hydrolase. This enzyme participates in benzoate degradation via hydroxylation. References * * EC 3.1.1 Enzymes of unknown structure {{3.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
