Image Aspartate transaminase.png thumb right 300px Aspartate transaminase from E. coli with Pyridoxal 5 Phosphate cofactor In biochemistry , a transaminase or an aminotransferase is an enzyme that catalyze s a type of reaction between an amino acid and an alpha keto acid &alpha keto acid . To be specific, this reaction transamination involves removing the amino group from the amino acid, leaving behind an keto acid, and transferring it to the reactant keto acid and converting it into an amino acid. Some transamination activities of the ribosome have been found to be catalyzed by so called ribozymes RNA enzymes . Examples being the hammerhead ribozyme , the VS ribozyme and the hairpin ribozyme . The transaminase enzymes are important in the production of various amino acids, and measuring the concentration s of various transaminases in the blood is important in the diagnosing and tracking many disease s. Transaminases require the coenzyme pyridoxal phosphate , which is converted into pyridoxamine in the first phase of the reaction, when an amino acid is converted into a keto acid. Enzyme bound pyridoxamine in turn reacts with pyruvate , oxaloacetate , or alpha ketoglutarate , giving alanine , aspartic acid , or glutamic acid , respectively. Many transamination reactions occur in tissues, catalysed by transaminases specific for a particular amino keto acid pair. The reactions are readily reversible, the direction being determined by which of the reactants are in excess. The specific enzymes are named from one of the reactant pairs, for example the reaction between glutamic acid and pyruvic acid to make alpha ketoglutaric acid and alanine is called glutamic pyruvic transaminase or GPT for short. Tissue transaminase activities can be investigated by incubating a homogenate ... GABA transaminase inhibitor References Ghany, Marc & Hoofnagle, Jay H. 2005 . Approach to the Patient ... fr Transaminase hr Transaminaze it Transaminasi ja pl Aminotransferazy pt Transaminase ... more details
enzyme Name dihydroxyphenylalanine transaminase EC number 2.6.1.49 CAS number 37277 98 8 IUBMB EC number 2 6 1 49 GO code 0047309 image width caption In enzymology , a dihydroxyphenylalanine transaminase EC number 2.6.1.49 is an enzyme that catalysis catalyzes the chemical reaction 3,4 dihydroxy L phenylalanine 2 oxoglutarate math rightleftharpoons math 3,4 dihydroxyphenylpyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 3,4 dihydroxy L phenylalanine and 2 oxoglutarate , whereas its two product chemistry products are 3,4 dihydroxyphenylpyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 3,4 dihydroxy L phenylalanine 2 oxoglutarate aminotransferase . Other names in common use include dopa transaminase , dihydroxyphenylalanine aminotransferase , aspartate DOPP transaminase ADT , L dopa transaminase , dopa aminotransferase , glutamate DOPP transaminase GDT , phenylalanine DOPP transaminase PDT , DOPA 2 oxoglutarate aminotransferase , and DOPAATS . This enzyme participates in tyrosine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Fonnum F, Larsen K date 1965 title Purification and properties of dihydroxyphenylalanine transaminase from guinea pig brain journal J. Neurochem. volume 12 pages 589&ndash 98 pmid 5829872 doi 10.1111 j.1471 4159.1965.tb04251.x issue 7 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name aminolevulinate transaminase EC number 2.6.1.43 CAS number 9012 46 8 IUBMB EC number 2 6 1 43 GO code 0047665 image width caption In enzymology , an aminolevulinate transaminase EC number 2.6.1.43 is an enzyme that catalysis catalyzes the chemical reaction 5 aminolevulinate pyruvate math rightleftharpoons math 4,5 dioxopentanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are 5 aminolevulinate and pyruvate , whereas its two product chemistry products are 4,5 dioxopentanoate and L alanine . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 5 aminolevulinate pyruvate aminotransferase . Other names in common use include aminolevulinate aminotransferase, gamma,delta dioxovalerate , aminotransferase , gamma,delta dioxovaleric acid transaminase , 4,5 dioxovalerate aminotransferase , 4,5 dioxovaleric acid transaminase , 4,5 dioxovaleric transaminase , 5 aminolevulinic acid transaminase , alanine gamma,delta dioxovalerate aminotransferase , alanine dioxovalerate aminotransferase , alanine 4,5 dioxovalerate aminotransferase , aminolevulinic acid transaminase , dioxovalerate transaminase , L alanine 4,5 dioxovalerate aminotransferase , L alanine 4,5 dioxovaleric acid transaminase , L alanine dioxovalerate transaminase , DOVA transaminase , and 4,5 dioxovaleric acid aminotransferase . This enzyme participates in porphyrin and chlorophyll metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Gibson KD, Matthew M and Neuberger A date 1961 title Biosynthesis of porphyrins and chlorophylls journal Nature volume 192 issue 4799 pages 204&ndash 208 doi 10.1038 192204a0 pmid 13898421 cite journal author NEUBERGER A, TURNER JM date 1963 title gamma,delta Dioxovalerate aminotransferase activity in Rhodopseudomonas spheroides journal Biochim. Biophys. Acta. volume 67 ... more details
enzyme Name diamine transaminase EC number 2.6.1.29 CAS number 9031 83 8 IUBMB EC number 2 6 1 29 GO code 0019161 image width caption In enzymology , a diamine transaminase EC number 2.6.1.29 is an enzyme that catalysis catalyzes the chemical reaction an alpha,omega diamine 2 oxoglutarate math rightleftharpoons math an omega aminoaldehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are alpha,omega diamine and 2 oxoglutarate , whereas its two product chemistry products are omega aminoaldehyde and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is diamine 2 oxoglutarate aminotransferase . Other names in common use include amine transaminase , amine ketoacid transaminase , diamine aminotransferase , and diamine ketoglutaric transaminase . This enzyme participates in urea cycle and metabolism of amino groups . References reflist 1 cite journal author Kim K date 1964 title Purification and properties of a diamine alpha ketoglutarate transaminase from Escherichia coli journal J. Biol. Chem. volume 239 pages 783&ndash 786 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name 2 aminoadipate transaminase EC number 2.6.1.39 CAS number 9033 00 5 IUBMB EC number 2 6 1 39 GO code 0047536 image width caption In enzymology , a 2 aminoadipate transaminase EC number 2.6.1.39 is an enzyme that catalysis catalyzes the chemical reaction L 2 aminoadipate 2 oxoglutarate math rightleftharpoons math 2 oxoadipate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L 2 aminoadipate and 2 oxoglutarate , whereas its two product chemistry products are 2 oxoadipate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L 2 aminoadipate 2 oxoglutarate aminotransferase . Other names in common use include alpha aminoadipate aminotransferase , 2 aminoadipate aminotransferase , 2 aminoadipic aminotransferase , glutamic ketoadipic transaminase , and glutamate alpha ketoadipate transaminase . This enzyme participates in lysine biosynthesis and lysine degradation . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 2DTV . References reflist 1 cite journal author Matsuda M, Ogur M date 1969 title Separation and specificity of the yeast glutamate alpha ketoadipate transaminase journal J. Biol. Chem. volume 244 pages 3352&ndash 8 pmid 5792664 issue 12 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name glycine transaminase EC number 2.6.1.4 CAS number 9032 99 9 IUBMB EC number 2 6 1 4 GO code 0047958 image width caption In enzymology , a glycine transaminase EC number 2.6.1.4 is an enzyme that catalysis catalyzes the chemical reaction glycine 2 oxoglutarate math rightleftharpoons math glyoxylate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are glycine and 2 oxoglutarate , whereas its two product chemistry products are glyoxylate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is glycine 2 oxoglutarate aminotransferase . Other names in common use include glutamic glyoxylic transaminase , glycine aminotransferase , glyoxylate glutamic transaminase , L glutamate glyoxylate aminotransferase , and glyoxylate glutamate aminotransferase . This enzyme participates in glycine, serine and threonine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Nakada HI year 1964 title Glutamic glycine transaminase from rat liver journal J. Biol. Chem. volume 239 pages 468&ndash 471 pmid 14169146 cite journal author Thompson JS and Richardson KE year 1966 title Isolation and chracterization of a glutamate glycine transaminase from human liver journal Arch. Biochem. Biophys. volume 117 issue 3 pages 599&ndash 603 doi 10.1016 0003 9861 66 90101 9 Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ... more details
enzyme Name leucine transaminase EC number 2.6.1.6 CAS number 9030 37 9 IUBMB EC number 2 6 1 6 GO code 0050048 image width caption In enzymology , a leucine transaminase EC number 2.6.1.6 is an enzyme that catalysis catalyzes the chemical reaction L leucine 2 oxoglutarate math rightleftharpoons math 4 methyl 2 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L leucine and 2 oxoglutarate , whereas its two product chemistry products are 4 methyl 2 oxopentanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L leucine 2 oxoglutarate aminotransferase . Other names in common use include L leucine aminotransferase , leucine 2 oxoglutarate transaminase , leucine aminotransferase , and leucine alpha ketoglutarate transaminase . This enzyme participates in 3 metabolism metabolic pathways valine, leucine and isoleucine degradation , valine, leucine and isoleucine biosynthesis , and pantothenate and coa biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Aki K, Ogawa K, Ichihara A date 1968 title Transaminases of branched chain amino acids. IV. Purification and properties of two enzymes from rat liver journal Biochim. Biophys. Acta. volume 159 pages 276&ndash 84 pmid 4968655 issue 2 cite journal author Ikeda T, Konishi Y, Ichihara A date 1976 title Transaminase of branched chain amino acids. XI. Leucine methionine transaminase of rat liver mitochondria journal Biochim. Biophys. Acta. volume 445 pages 622&ndash 31 pmid 974100 issue 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name S 3 amino 2 methylpropionate transaminase EC number 2.6.1.22 CAS number 9031 95 2 IUBMB EC number 2 6 1 22 GO code 0047298 image width caption In enzymology , a S 3 amino 2 methylpropionate transaminase EC number 2.6.1.22 is an enzyme that catalysis catalyzes the chemical reaction S 3 amino 2 methylpropanoate 2 oxoglutarate math rightleftharpoons math 2 methyl 3 oxopropanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are S 3 amino 2 methylpropanoate and 2 oxoglutarate , whereas its two product chemistry products are 2 methyl 3 oxopropanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is S 3 amino 2 methylpropanoate 2 oxoglutarate aminotransferase . Other names in common use include L 3 aminoisobutyrate transaminase , beta aminobutyric transaminase , L 3 aminoisobutyric aminotransferase , and beta aminoisobutyrate alpha ketoglutarate transaminase . This enzyme participates in valine, leucine and isoleucine degradation . References reflist 1 cite journal author Kakimoto Y, Kanazawa A, Taniguchi K, Sano I date 1968 title Beta aminoisobutyrate alpha ketoglutarate transaminase in relation to beta aminoisobutyric aciduria journal Biochim. Biophys. Acta. volume 156 pages 374&ndash 80 pmid 5641913 issue 2 cite journal author Tamaki N, Sakata SF, Matsuda K date 2000 title Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver journal Methods Enzymol. volume 324 pages 376&ndash 89 pmid 10989446 doi 10.1016 S0076 6879 00 24247 X series Methods in Enzymology isbn 9780121822255 Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
enzyme Name 5 aminovalerate transaminase EC number 2.6.1.48 CAS number 37277 97 7 IUBMB EC number 2 6 1 48 GO code 0047589 image width caption In enzymology , a 5 aminovalerate transaminase EC number 2.6.1.48 is an enzyme that catalysis catalyzes the chemical reaction 5 aminopentanoate 2 oxoglutarate math rightleftharpoons math 5 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 5 aminopentanoate and 2 oxoglutarate , whereas its two product chemistry products are 5 oxopentanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 5 aminopentanoate 2 oxoglutarate aminotransferase . Other names in common use include 5 aminovalerate aminotransferase , delta aminovalerate aminotransferase , and delta aminovalerate transaminase . This enzyme participates in lysine degradation . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Ichihara A, Ichihara EA and Suda M date Tokyo title Metabolism of L lysine by bacterial enzymes. IV. delta Aminovaleric acid glutamic acid transaminase journal J. volume Biochem. pages 412&ndash 420 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name succinyldiaminopimelate transaminase EC number 2.6.1.17 CAS number 9030 46 0 IUBMB EC number 2 6 1 17 GO code 0009016 image width caption In enzymology , a succinyldiaminopimelate transaminase EC number 2.6.1.17 is an enzyme that catalysis catalyzes the chemical reaction N succinyl L 2,6 diaminoheptanedioate 2 oxoglutarate math rightleftharpoons math N succinyl L 2 amino 6 oxoheptanedioate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N succinyl L 2,6 diaminoheptanedioate and 2 oxoglutarate , whereas its two product chemistry products are N succinyl L 2 amino 6 oxoheptanedioate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is N succinyl L 2,6 diaminoheptanedioate 2 oxoglutarate aminotransferase . Other names in common use include succinyldiaminopimelate aminotransferase , and N succinyl L diaminopimelic glutamic transaminase . This enzyme participates in lysine biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Peterkofsky B and Gilvarg C date 1961 title N Succinyl L diaminopimelic glutamic transaminase journal J. Biol. Chem. volume 236 pages 1432&ndash 1438 pmid 13734750 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name diiodotyrosine transaminase EC number 2.6.1.24 CAS number 9033 18 5 IUBMB EC number 2 6 1 24 GO code 0047861 image width caption In enzymology , a diiodotyrosine transaminase EC number 2.6.1.24 is an enzyme that catalysis catalyzes the chemical reaction 3,5 diiodo L tyrosine 2 oxoglutarate math rightleftharpoons math 4 hydroxy 3,5 diiodophenylpyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 3,5 diiodo L tyrosine and 2 oxoglutarate , whereas its two product chemistry products are 4 hydroxy 3,5 diiodophenylpyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 3,5 diiodo L tyrosine 2 oxoglutarate aminotransferase . Other names in common use include diiodotyrosine aminotransferase , halogenated tyrosine aminotransferase , and halogenated tyrosine transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Nakano M year 1967 title Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney mitochondria journal J. Biol. Chem. volume 242 pages 73&ndash 81 pmid 4381052 issue 1 cite journal author Nakano M and Danowski TS year 1964 title Thyroid hormone transaminase and oxidase in rat kidney mitochondria journal Biochim. Biophys. Acta volume 85 pages 18&ndash 28 pmid 14159298 Transaminases Thyroid hormone metabolism enzymes and transporters Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ja ... more details
enzyme Name tryptophan transaminase EC number 2.6.1.27 CAS number 9022 98 4 IUBMB EC number 2 6 1 27 GO code 0050362 image width caption In enzymology , a tryptophan transaminase EC number 2.6.1.27 is an enzyme that catalysis catalyzes the chemical reaction L tryptophan 2 oxoglutarate math rightleftharpoons math indol 3 yl pyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L tryptophan and 2 oxoglutarate , whereas its two product chemistry products are indol 3 yl pyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L tryptophan 2 oxoglutarate aminotransferase . Other names in common use include L phenylalanine 2 oxoglutarate aminotransferase , tryptophan aminotransferase , 5 hydroxytryptophan ketoglutaric transaminase , hydroxytryptophan aminotransferase , L tryptophan aminotransferase , and L tryptophan transaminase . This enzyme participates in tryptophan metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author George H, Gabay S year 1968 title Brain aromatic aminotransferase. I. Purification and some properties of pig brain L phenylalanine 2 oxoglutarate aminotransferase journal Biochim. Biophys. Acta. volume 167 pages 555&ndash 66 pmid 5722279 issue 3 cite journal author O Neil SR, DeMoss RD year 1968 title Tryptophan transaminase from Clostridium sporogenes journal Arch. Biochem. Biophys. volume 127 pages 361&ndash 9 pmid 5697992 doi 10.1016 0003 9861 68 90237 3 issue 1 cite journal author Tangen O, Fonnum F and Haavaldsen R year 1965 title Separation and purification of aromatic amino acid transaminases from rat brain journal Biochim. Biophys. Acta volume 96 pages 82&ndash 90 pmid 14285270 Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure transferase stub ... more details
protein Name glutamic pyruvate transaminase caption image width HGNCid 4552 Symbol GPT AltSymbols EntrezGene 2875 OMIM 138200 RefSeq NM 005309 UniProt P24298 PDB ECnumber 2.6.1.2 Chromosome 8 Arm q Band 24.2 LocusSupplementaryData qter infobox enzyme Name Alanine transaminase EC number 2.6.1.2 CAS number 9000 86 6 IUBMB EC number 2 6 1 2 GO code 0004021 image width caption Alanine transaminase or ALT is a transaminase enzyme EC number 2.6.1.2 . It is also called serum glutamic pyruvic transaminase SGPT or alanine aminotransferase ALAT . ALT is found in blood plasma serum and in various bodily tissues, but is most commonly associated with the liver . It catalyzes the two parts of the alanine cycle . Function It catalyzes the transfer of an amino group from alanine to Alpha Ketoglutaric acid ketoglutarate , the products of this reversible transamination reaction being pyruvate and glutamate . glutamate pyruvate unicode & 8652 alpha ketoglutaric acid ketoglutarate alanine Image Alanine amino transf rase.png thumb none 600px Alanine transaminase Clinical significance It is commonly measured clinically as a part of a diagnostic evaluation of Liver function tests hepatocellular injury , to determine liver health. When used in diagnostics, it is almost always measured in international units liter U L . ref name Wang2012 cite journal last1 Wang first1 CS year 2012 title Impact of increasing ... transaminase shows a marked diurnal variation . Elevated levels class wikitable Patient type ... Liver Transaminase Levels in the Asymptomatic Patient , American Family Physician . ref When elevated ... ref See also Aspartate transaminase Liver function tests References reflist External links MeshName Alanine transaminase http www.nlm.nih.gov medlineplus ency article 003473.htm ALT MedlinePlus ... DEFAULTSORT Alanine Transaminase Category Biomarkers Category Liver function tests Category Enzymes ... amino transf rase hr Alanin transaminaza id Alanina transaminase it Alanina transaminasi nl Alanine ... more details
enzyme Name 2,5 diaminovalerate transaminase EC number 2.6.1.8 CAS number 9030 39 1 IUBMB EC number 2 6 1 8 GO code 0047531 image width caption In enzymology , a 2,5 diaminovalerate transaminase EC number 2.6.1.8 is an enzyme that catalysis catalyzes the chemical reaction 2,5 diaminopentanoate 2 oxoglutarate math rightleftharpoons math 5 amino 2 oxopentanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 2,5 diaminopentanoate and 2 oxoglutarate , whereas its two product chemistry products are 5 amino 2 oxopentanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 2,5 diaminopentanoate 2 oxoglutarate aminotransferase . Other names in common use include diamino acid transaminase , and diamino acid aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author ROBERTS E date 1954 title Studies of transamination journal Arch. Biochem. Biophys. volume 48 pages 395&ndash 401 pmid 13125615 doi 10.1016 0003 9861 54 90355 0 issue 2 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name 2 aminohexanoate transaminase EC number 2.6.1.67 CAS number 111310 35 1 IUBMB EC number 2 6 1 67 GO code 0047537 image width caption In enzymology , a 2 aminohexanoate transaminase EC number 2.6.1.67 is an enzyme that catalysis catalyzes the chemical reaction L 2 aminohexanoate 2 oxoglutarate math rightleftharpoons math 2 oxohexanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L 2 aminohexanoate and 2 oxoglutarate , whereas its two product chemistry products are 2 oxohexanoate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L 2 aminohexanoate 2 oxoglutarate aminotransferase . Other names in common use include norleucine transaminase , norleucine leucine aminotransferase , and leucine L norleucine 2 oxoglutarate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Der Garabedian PA, Vermeersch JJ date 1987 title Candida L norleucine,leucine 2 oxoglutarate aminotransferase Purification and properties journal Eur. J. Biochem. volume 167 pages 141&ndash 7 pmid 3622507 doi 10.1111 j.1432 1033.1987.tb13315.x issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name 4 hydroxyglutamate transaminase EC number 2.6.1.23 CAS number 37277 86 4 IUBMB EC number 2 6 1 23 GO code 0047578 image width caption In enzymology , a 4 hydroxyglutamate transaminase EC number 2.6.1.23 is an enzyme that catalysis catalyzes the chemical reaction 4 hydroxy L glutamate 2 oxoglutarate math rightleftharpoons math 4 hydroxy 2 oxoglutarate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are 4 hydroxy L glutamate and 2 oxoglutarate , whereas its two product chemistry products are 4 hydroxy 2 oxoglutarate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is 4 hydroxy L glutamate 2 oxoglutarate aminotransferase . This enzyme is also called 4 hydroxyglutamate aminotransferase . This enzyme participates in arginine and proline metabolism . References reflist 1 cite journal author GOLDSTONE A, ADAMS E date 1962 title Metabolism of gamma hydroxyglutamic acid. I. Conversion to alpha hydroxy gamma ketoglutarate by purified glutamic aspartic transaminase to rat liver journal J. Biol. Chem. volume 237 pages 3476&ndash 85 pmid 13948827 cite journal author KURATOMI K, FUKUNAGA K, KOBAYASHI Y date 1963 title THE METABOLISM OF GAMMA HYDROXYGLUTAMATE IN RAT LIVER. II. A TRANSAMINASE CONCERNED IN GAMMA HYDROXYGLUTAMATE METABOLISM journal Biochim. Biophys. Acta. volume 78 pages 629&ndash 36 pmid 14089443 doi 10.1016 0006 3002 63 91028 X issue 4 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name acetylornithine transaminase EC number 2.6.1.11 CAS number 9030 40 4 IUBMB EC number 2 6 1 11 GO code 0003992 image width caption In enzymology , an acetylornithine transaminase EC number 2.6.1.11 is an enzyme that catalysis catalyzes the chemical reaction N sub 2 sub acetyl L ornithine 2 oxoglutarate math rightleftharpoons math N acetyl L glutamate 5 semialdehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N2 acetyl L ornithine and 2 oxoglutarate , whereas its two product chemistry products are N acetyl L glutamate 5 semialdehyde and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is N2 acetyl L ornithine 2 oxoglutarate 5 aminotransferase . Other names in common use include acetylornithine delta transaminase , ACOAT , acetylornithine 5 aminotransferase , acetylornithine aminotransferase , N acetylornithine aminotransferase , N acetylornithine delta transaminase , N2 acetylornithine 5 transaminase , N2 acetyl L ornithine 2 oxoglutarate aminotransferase , succinylornithine aminotransferase , and 2 N acetyl L ornithine 2 oxoglutarate 5 aminotransferase . This enzyme participates in urea cycle and metabolism of amino groups . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1VEF , PDB link 1WKG , PDB link 1WKH , PDB link 2E54 , PDB link 2EH6 , and PDB link 2ORD . References reflist 1 cite journal author ALBRECHT AM, VOGEL HJ date 1964 title ACETYLORNITHINE DELTA TRANSAMINASE. PARTIAL PURIFICATION AND REPRESSION BEHAVIOR journal J. Biol. Chem. volume 239 pages 1872&ndash 6 pmid 14213368 cite journal author Vogel HJ date 1953 title Path of Ornithine Synthesis in Escherichia Coli journal Proc. Natl. Acad. Sci. U. S. A. volume ... more details
enzyme Name histidine transaminase EC number 2.6.1.38 CAS number 37277 92 2 IUBMB EC number 2 6 1 38 GO code 0008110 image width caption In enzymology , a histidine transaminase EC number 2.6.1.38 is an enzyme that catalysis catalyzes the chemical reaction L histidine 2 oxoglutarate math rightleftharpoons math imidazol 5 yl pyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L histidine and 2 oxoglutarate , whereas its two product chemistry products are imidazol 5 yl pyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L histidine 2 oxoglutarate aminotransferase . Other names in common use include histidine aminotransferase , and histidine 2 oxoglutarate aminotransferase . This enzyme participates in histidine metabolism . References reflist 1 cite journal author Coote JG, Hassall H date 1969 title The role of imidazol 5 yl lactate nicotinamide adenine dinucleotide phosphate oxidoreductase and histidine 2 oxoglutarate aminotransferase in the degradation of imidazol 5 yl lactate by Pseudomonas acidovorans journal Biochem. J. volume 111 pages 237&ndash 9 pmid 4303364 issue 2 pmc 1187811 cite journal author Wickremasinghe R, Hedegaard J and Roche J date 1967 title Degradation de la L histidine chez Escherichia coli B formation de l acide imidazolepyruvique par une histidine transaminase journal C.R. Soc. Biol. volume 161 pages 1891&ndash 1896 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name cysteine transaminase EC number 2.6.1.3 CAS number 9030 32 4 IUBMB EC number 2 6 1 3 GO code 0047801 image width caption In enzymology , a cysteine transaminase EC number 2.6.1.3 is an enzyme that catalysis catalyzes the chemical reaction L cysteine 2 oxoglutarate math rightleftharpoons math mercaptopyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L cysteine and 2 oxoglutarate , whereas its two product chemistry products are mercaptopyruvate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is L cysteine 2 oxoglutarate aminotransferase . Other names in common use include cysteine aminotransferase , L cysteine aminotransferase , and CGT . This enzyme participates in cysteine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author CHATAGNER F, SAURET IGNAZI G date Paris title Role of transamination and pyridoxal phosphate in the enzymatic formation of hydrogen sulfide from cysteine by the rat liver under anaerobiosis. journal Bull. Soc. Chim. volume Biol. pages 415&ndash 28 pmid 13342749 issue 2 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ja ... more details
enzyme Name D 4 hydroxyphenylglycine transaminase EC number 2.6.1.72 CAS number 117444 05 0 IUBMB EC number 2 6 1 72 GO code 0047320 image width caption In enzymology , a D 4 hydroxyphenylglycine transaminase EC number 2.6.1.72 is an enzyme that catalysis catalyzes the chemical reaction D 4 hydroxyphenylglycine 2 oxoglutarate math rightleftharpoons math 4 hydroxyphenylglyoxylate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are D 4 hydroxyphenylglycine and 2 oxoglutarate , whereas its two product chemistry products are 4 hydroxyphenylglyoxylate and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is D 4 hydroxyphenylglycine 2 oxoglutarate aminotransferase . This enzyme is also called D hydroxyphenylglycine aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Probst C, Grotz M, Krettek C, Pape HC date 2005 title Impact of hypothermia on the immunologic response after trauma and elective surgery journal Surg. Technol. Int. volume 14 pages 41&ndash 50 pmid 16525953 cite journal author Probst C, Grotz M, Krettek C, Pape HC date 2005 title Impact of hypothermia on the immunologic response after trauma and elective surgery journal Surg. Technol. Int. volume 14 pages 41&ndash 50 pmid 16525953 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose transaminase EC number 2.6.1.34 CAS number 37277 89 7 IUBMB EC number 2 6 1 34 GO code 0047302 image width caption In enzymology , an UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose transaminase EC number 2.6.1.34 is an enzyme that catalysis catalyzes the chemical reaction UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose 2 oxoglutarate math rightleftharpoons math UDP 2 acetamido 4 dehydro 2,6 dideoxyglucose L glutamate Thus, the two substrate biochemistry substrates of this enzyme are UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose and 2 oxoglutarate , whereas its two product chemistry products are UDP 2 acetamido 4 dehydro 2,6 dideoxyglucose and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is UDP 2 acetamido 4 amino 2,4,6 trideoxyglucose 2 oxoglutarate aminotransferase . Other names in common use include uridine diphospho 4 amino 2 acetamido 2,4,6 trideoxyglucose , and aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Distler J, Kaufman B, Roseman S date 1966 title Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae journal Arch. Biochem. Biophys. volume 116 pages 466&ndash 78 pmid 4381351 doi 10.1016 0003 9861 66 90054 3 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name aspartate transaminase EC number 2.6.1.1 CAS number 9000 97 9 IUBMB EC number 2 6 1 1 GO code 0004069 image Aspartate transaminase.png width caption Aspartate aminotransferase from E. coli Escherichia coli bound with cofactor Pyridoxal phosphate pyridoxal 5 phosphate . ref name pmid7909946 PDB 1AAM cite journal author Almo SC, Smith DL, Danishefsky AT, Ringe D title The structural basis ... doi 10.1093 protein 7.3.405 url issn ref Aspartate transaminase AST , also called aspartate aminotransferase AspAT ASAT AAT or serum glutamic oxaloacetic transaminase SGOT , is a pyridoxal phosphate PLP dependent transaminase enzyme EC number 2.6.1.1 . AST catalyzes the reversible transfer of an ... measured clinically as a marker for liver health. Function Aspartate transaminase ... 450px Reaction catalyzed by aspartate aminotransferase As a prototypical transaminase, AST relies ... of an aromatic amino acid transaminase EC number 2.6.1.57 . ref name pmid15983 cite journal author ... of aspartate transaminase from chicken heart mitochondria X ray crystallography studies have been performed to determine the structure of aspartate transaminase from various sources, including chicken ... Aspartate transaminase, as with all transaminases, operates via dual substrate recognition that is, it is able ... pmid 15889412 doi 10.1002 tcr.20042 pmc url ref In either case, the transaminase reaction consists of two ... 12488449 ref Clinical significance AST is similar to alanine transaminase ALT in that both enzymes ... Transaminases Alanine transaminase References reflist Further reading cite book last1 Jansonius first1 ... 7801 year 1991 pmid 1868057 doi 10.1021 bi00245a019 External links MeshName Aspartate Transaminase http ... Aspartate Transaminase Category Liver function tests Category EC 2.6.1 de Aspartat Aminotransferase ... transaminase it Aspartato transaminasi nl Aspartaat aminotransferase ja pl Aminotransferaza asparaginianowa pt Transaminase glut mico oxalac tica ru fi ... more details
enzyme Name succinylornithine transaminase EC number 2.6.1.81 CAS number IUBMB EC number 2 6 1 81 GO code 0043825 image width caption Orphan date February 2009 In enzymology , a succinylornithine transaminase EC number 2.6.1.81 is an enzyme that catalysis catalyzes the chemical reaction N sub 2 sub succinyl L ornithine 2 oxoglutarate math rightleftharpoons math N succinyl L glutamate 5 semialdehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are N2 succinyl L ornithine and 2 oxoglutarate , whereas its two product chemistry products are N succinyl L glutamate 5 semialdehyde and L glutamate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is N2 succinyl L ornithine 2 oxoglutarate 5 aminotransferase . Other names in common use include succinylornithine aminotransferase , N2 succinylornithine 5 aminotransferase , AstC , SOAT , and 2 N succinyl L ornithine 2 oxoglutarate 5 aminotransferase . This enzyme participates in arginine and proline metabolism . References reflist 1 cite journal author Vander Wauven C, Stalon V date 1985 title Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia journal J. Bacteriol. volume 164 pages 882&ndash 6 pmid 2865249 issue 2 pmc 214334 cite journal author Schneider BL, Kiupakis AK, Reitzer LJ date 1998 title Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli journal J. Bacteriol. volume 180 pages 4278&ndash 86 pmid 9696779 issue 16 pmc 107427 cite journal author Cunin R, Glansdorff N, Pierard A, Stalon V date 1986 title Biosynthesis and metabolism of arginine in bacteria journal Microbiol. Rev. volume 50 pages 314&ndash 52 pmid 3534538 issue 3 pmc 373073 cite journal author Itoh Y date 1997 title Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa ... more details
A GABA transaminase inhibitor is an enzyme inhibitor that acts upon GABA transaminase . Examples include vigabatrin ref name pmid18412635 cite journal author Wang QP, Jammoul F, Duboc A, et al title Treatment of epilepsy the GABA transaminase inhibitor, vigabatrin, induces neuronal plasticity in the mouse retina journal Eur. J. Neurosci. volume 27 issue 8 pages 2177 87 year 2008 month April pmid 18412635 pmc 2933832 doi 10.1111 j.1460 9568.2008.06175.x url http www3.interscience.wiley.com resolve openurl?genre article&sid nlm pubmed&issn 0953 816X&date 2008&volume 27&issue 8&spage 2177 ref , phenylethylidenehydrazine and Ethanolamine O sulfate ethanolamine O sulfate EOS . Certain members of this class are used as anticonvulsant s. There is some evidence that Melissa officinalis lemon balm inhibits GABA transaminase. ref http www.ingentaconnect.com content nrc cjpp 2007 00000085 00000009 art00015 ref References reflist GABA agonists and antagonists Anticonvulsants Enzyme inhibition Category GABA transaminase inhibitors ... more details
Encyclopedia
top
