enzyme Name Arginine pyruvate transaminase EC number 2.6.1.84 CAS number IUBMB EC number 2 6 1 84 GO code image width caption Orphan date February 2009 In enzymology , an arginine pyruvate transaminase EC number 2.6.1.84 is an enzyme that catalysis catalyzes the chemical reaction L arginine pyruvate math rightleftharpoons math 5 guanidino 2 oxopentanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L arginine and pyruvate , whereas its two product chemistry products are 5 guanidino 2 oxopentanoate 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 L arginine pyruvate aminotransferase . Other names in common use include arginine pyruvate transaminase , and AruH . References reflist 1 cite journal author Yang Z, Lu CD date 2007 title Characterization of an arginine pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1 journal J. Bacteriol. volume 189 pages 3954&ndash 9 pmid 17416668 doi 10.1128 JB.00262 07 issue 11 pmc 1913410 cite journal author Yang Z, Lu CD date 2007 title Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa journal J. Bacteriol. volume 189 pages 3945&ndash 53 pmid 17416670 doi 10.1128 JB.00261 07 issue 11 pmc 1913404 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name pyridoxamine phosphate transaminase EC number 2.6.1.54 CAS number 9074 84 4 IUBMB EC number 2 6 1 54 GO code 0019163 image width caption In enzymology , a pyridoxamine phosphate transaminase EC number 2.6.1.54 is an enzyme that catalysis catalyzes the chemical reaction pyridoxamine 5 phosphate 2 oxoglutarate math rightleftharpoons math pyridoxal 5 phosphate D glutamate Thus, the two substrate biochemistry substrates of this enzyme are pyridoxamine 5 phosphate and 2 oxoglutarate , whereas its two product chemistry products are pyridoxal 5 phosphate and D 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 pyridoxamine 5 phosphate 2 oxoglutarate aminotransferase D glutamate forming . Other names in common use include pyridoxamine phosphate aminotransferase , pyridoxamine 5 phosphate alpha ketoglutarate transaminase , and pyridoxamine 5 phosphate transaminase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . References reflist 1 cite journal author Tani Y, Ukita M and Ogata K date 1972 title Studies on vitamin B6 metabolism in microorganisms. Part X. Further purification and characterization of pyridoxamine 5 phosphate alpha ketoglutarate transaminase from Clostridium kainantoi journal Agric. Biol. Chem. volume 36 pages 181&ndash 188 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name alanine oxomalonate transaminase EC number 2.6.1.47 CAS number 37277 96 6 IUBMB EC number 2 6 1 47 GO code 0047308 image width caption In enzymology , an alanine oxomalonate transaminase EC number 2.6.1.47 is an enzyme that catalysis catalyzes the chemical reaction L alanine oxomalonate math rightleftharpoons math pyruvate aminomalonate Thus, the two substrate biochemistry substrates of this enzyme are L alanine and oxomalonate , whereas its two product chemistry products are pyruvate and aminomalonate . 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 alanine oxomalonate aminotransferase . Other names in common use include alanine oxomalonate aminotransferase , L alanine ketomalonate transaminase , and alanine ketomalonate mesoxalate transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Nagayama H, Muramatsu M and Shimura K date 1958 title Enzymatic formation of aminomalonic acid from ketomalonic acid journal Nature volume 181 issue 4606 pages 417&ndash 418 doi 10.1038 181417a0 pmid 13504217 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name dTDP 4 amino 4,6 dideoxygalactose transaminase EC number 2.6.1.59 CAS number 72560 97 5 IUBMB EC number 2 6 1 59 GO code 0019180 image width caption lowercase In enzymology , a dTDP 4 amino 4,6 dideoxygalactose transaminase EC number 2.6.1.59 is an enzyme that catalysis catalyzes the chemical reaction dTDP 4 amino 4,6 dideoxy D galactose 2 oxoglutarate math rightleftharpoons math dTDP 4 dehydro 6 deoxy D galactose L glutamate Thus, the two substrate biochemistry substrates of this enzyme are dTDP 4 amino 4,6 dideoxy D galactose and 2 oxoglutarate , whereas its two product chemistry products are dTDP 4 dehydro 6 deoxy D galactose 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 dTDP 4,6 dideoxy D galactose 2 oxoglutarate aminotransferase . Other names in common use include thymidine diphosphoaminodideoxygalactose aminotransferase , and thymidine diphosphate 4 keto 6 deoxy D glucose transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Oashi H, Matsuhashi M, Matsuhashi S date 1971 title Thymidine diphosphate 4 acetamido 4,6 dideoxyhexoses. IV Purification and properties of thymidine diphosphate 4 keto 6 deoxy D glucose transaminase from Pasteurella pseudotuberculosis journal J. Biol. Chem. volume 246 pages 2325&ndash 30 pmid 4928644 issue 8 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name glutamine scyllo inositol transaminase EC number 2.6.1.50 CAS number 9033 03 8 IUBMB EC number 2 6 1 50 GO code 0047310 image width caption In enzymology , a glutamine scyllo inositol transaminase EC number 2.6.1.50 is an enzyme that catalysis catalyzes the chemical reaction L glutamine 2,4,6 3,5 pentahydroxycyclohexanone math rightleftharpoons math 2 oxoglutaramate 1 amino 1 deoxy scyllo inositol Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and 2,4,6 3,5 pentahydroxycyclohexanone , whereas its two product chemistry products are 2 oxoglutaramate and 1 amino 1 deoxy scyllo inositol . 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 glutamine 2,4,6 3,5 pentahydroxycyclohexanone aminotransferase . Other names in common use include glutamine scyllo inosose aminotransferase , L glutamine keto scyllo inositol aminotransferase , glutamine scyllo inosose transaminase , and L glutamine scyllo inosose transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Walker JB, Walker MS date 1969 title Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines journal Biochemistry. volume 8 pages 763&ndash 70 pmid 5781017 doi 10.1021 bi00831a003 issue 3 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name pyridoxamine pyruvate transaminase EC number 2.6.1.30 CAS number 9023 38 5 IUBMB EC number 2 6 1 30 GO code 0047300 image width caption In enzymology , a pyridoxamine pyruvate transaminase EC number 2.6.1.30 is an enzyme that catalysis catalyzes the chemical reaction pyridoxamine pyruvate math rightleftharpoons math pyridoxal L alanine Thus, the two substrate biochemistry substrates of this enzyme are pyridoxamine and pyruvate , whereas its two product chemistry products are pyridoxal 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 pyridoxamine pyruvate aminotransferase . This enzyme is also called pyridoxamine pyruvic transaminase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . References reflist 1 cite journal author Wada H and Snell EE date 1962 title Enzymatic transamination of pyridoxamine. II. Crystalline pyridoxamine pyruvate transaminase journal J. Biol. Chem. volume 237 pages 133&ndash 137 pmid 14004227 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name valine 3 methyl 2 oxovalerate transaminase EC number 2.6.1.32 CAS number 9023 14 7 IUBMB EC number 2 6 1 32 GO code 0047301 image width caption In enzymology , a valine 3 methyl 2 oxovalerate transaminase EC number 2.6.1.32 is an enzyme that catalysis catalyzes the chemical reaction L valine S 3 methyl 2 oxopentanoate math rightleftharpoons math 3 methyl 2 oxobutanoate L isoleucine Thus, the two substrate biochemistry substrates of this enzyme are L valine and S 3 methyl 2 oxopentanoate , whereas its two product chemistry products are 3 methyl 2 oxobutanoate and L isoleucine . 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 valine S 3 methyl 2 oxopentanoate aminotransferase . Other names in common use include valine isoleucine transaminase , valine 3 methyl 2 oxovalerate aminotransferase , alanine valine transaminase , valine 2 keto methylvalerate aminotransferase , and valine isoleucine aminotransferase . References reflist 1 cite journal last Kagan first Z. S. coauthors A. S. Dronov and V. L. Kretovich year 1968 trans title Some properties of valine isoleucine and valine glutamate aminotransferases of pea sprouts language Russian journal Doklady Akademii Nauk SSSR volume 179 pages 1236&ndash 1239 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name valine pyruvate transaminase EC number 2.6.1.66 CAS number 132421 38 6 IUBMB EC number 2 6 1 66 GO code 0009042 image width caption In enzymology , a valine pyruvate transaminase EC number 2.6.1.66 is an enzyme that catalysis catalyzes the chemical reaction L valine pyruvate math rightleftharpoons math 3 methyl 2 oxobutanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L valine and pyruvate , whereas its two product chemistry products are 3 methyl 2 oxobutanoate 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 L valine pyruvate aminotransferase . Other names in common use include transaminase C , valine pyruvate aminotransferase , and alanine oxoisovalerate aminotransferase . This enzyme participates in valine, leucine and isoleucine biosynthesis . References reflist 1 cite journal author Falkinham JO 3rd date 1979 title Identification of a mutation affecting an alanine alpha ketoisovalerate transaminase activity in Escherichia coli K 12 journal Mol. Gen. Genet. volume 176 pages 147&ndash 9 pmid 396446 doi 10.1007 BF00334306 issue 1 cite journal author RUDMAN D, MEISTER A date 1953 title Transamination in Escherichia coli journal J. Biol. Chem. volume 200 pages 591&ndash 604 pmid 13034817 issue 2 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name histidinol phosphate transaminase EC number 2.6.1.9 CAS number 9032 98 8 IUBMB EC number 2 6 1 9 GO code 0004400 image width caption In enzymology , a histidinol phosphate transaminase EC number 2.6.1.9 is an enzyme that catalysis catalyzes the chemical reaction L histidinol phosphate 2 oxoglutarate math rightleftharpoons math 3 imidazol 4 yl 2 oxopropyl phosphate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L histidinol phosphate and 2 oxoglutarate , whereas its two product chemistry products are 3 imidazol 4 yl 2 oxopropyl phosphate 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 histidinol phosphate 2 oxoglutarate aminotransferase . Other names in common use include imidazolylacetolphosphate transaminase , glutamic imidazoleacetol phosphate transaminase , histidinol phosphate aminotransferase , imidazoleacetol phosphate transaminase , L histidinol phosphate aminotransferase , histidine imidazoleacetol phosphate transaminase , IAP transaminase , and imidazolylacetolphosphate aminotransferase . This enzyme participates in 5 metabolism metabolic pathways histidine metabolism , tyrosine metabolism , phenylalanine metabolism , phenylalanine, tyrosine and tryptophan biosynthesis , and novobiocin biosynthesis . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 11 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FG3 , PDB link 1FG7 , PDB link 1GEW , PDB link 1GEX , PDB link 1GEY , PDB link 1H1C , PDB link 1IJI , PDB link 1UU0 , PDB link 1UU1 , PDB link 1UU2 , and PDB link 2F8J . References reflist 1 cite journal author AMES BN, HORECKER BL year 1956 title The biosynthesis of histidine imidazoleacetol phosphate transaminase journal J. Biol. Chem. volume 220 pages ... more details
enzyme Name glutamine phenylpyruvate transaminase EC number 2.6.1.64 CAS number 68518 06 9 IUBMB EC number 2 6 1 64 GO code 0047316 image width caption In enzymology , a glutamine phenylpyruvate transaminase EC number 2.6.1.64 is an enzyme that catalysis catalyzes the chemical reaction L glutamine phenylpyruvate math rightleftharpoons math 2 oxoglutaramate L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and phenylpyruvate , whereas its two product chemistry products are 2 oxoglutaramate and L phenylalanine . This enzyme belongs to the family of transferase s, to be specific, the transaminases , that transfer nitrogenous groups. The systematic name of this enzyme class is L glutamine phenylpyruvate aminotransferase . Other names in common use include glutamine transaminase K , and glutamine phenylpyruvate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1YIY and PDB link 1YIZ . References reflist 1 cite journal author Cooper AJ date 1978 title Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L phenylalanine and alpha keto gamma methiolbutyrate journal Anal. Biochem. volume 89 pages 451&ndash 60 pmid 727444 doi 10.1016 0003 2697 78 90374 3 issue 2 cite journal author Cooper AJ, Meister A date 1974 title Isolation and properties of a new glutamine transaminase from rat kidney journal J. Biol. Chem. volume 249 pages 2554&ndash 61 pmid 4822504 issue 8 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name glutamine pyruvate transaminase EC number 2.6.1.15 CAS number 9030 44 8 IUBMB EC number 2 6 1 15 GO code 0047945 image width caption In enzymology , a glutamine pyruvate transaminase EC number 2.6.1.15 is an enzyme that catalysis catalyzes the chemical reaction L glutamine pyruvate math rightleftharpoons math 2 oxoglutaramate L alanine Thus, the two substrate biochemistry substrates of this enzyme are L glutamine and pyruvate , whereas its two product chemistry products are 2 oxoglutaramate 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 L glutamine pyruvate aminotransferase . Other names in common use include glutaminase II , L glutamine transaminase L , and glutamine oxo acid transaminase . This enzyme participates in glutamate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1V2D , PDB link 1V2E , and PDB link 1V2F . References reflist 1 cite journal author Cooper JL, Meister A date 1972 title Isolation and properties of highly purified glutamine transaminase journal Biochemistry. volume 11 pages 661&ndash 71 pmid 5059882 doi 10.1021 bi00755a001 issue 5 cite journal author MEISTER A date 1954 title Studies on the mechanism and specificity of the glutamine alpha keto acid transamination deamidation reaction journal J. Biol. Chem. volume 210 pages 17&ndash 35 pmid 13201566 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of known structure ... more details
enzyme Name R 3 amino 2 methylpropionate pyruvate transaminase EC number 2.6.1.40 CAS number 37279 00 8 IUBMB EC number 2 6 1 40 GO code 0047305 image width caption In enzymology , a R 3 amino 2 methylpropionate pyruvate transaminase EC number 2.6.1.40 is an enzyme that catalysis catalyzes the chemical reaction R 3 amino 2 methylpropanoate pyruvate math rightleftharpoons math 2 methyl 3 oxopropanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are R 3 amino 2 methylpropanoate and pyruvate , whereas its two product chemistry products are 2 methyl 3 oxopropanoate 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 R 3 amino 2 methylpropanoate pyruvate aminotransferase . Other names in common use include D 3 aminoisobutyrate pyruvate transaminase , beta aminoisobutyrate pyruvate aminotransferase , D 3 aminoisobutyrate pyruvate aminotransferase , D 3 aminoisobutyrate pyruvate transaminase , R 3 amino 2 methylpropionate transaminase , and D beta aminoisobutyrate pyruvate aminotransferase . References reflist 1 cite journal author Kakimoto Y, Taniguchi K, Sano I year 1969 title D beta aminoisobutyrate pyruvate aminotransferase in mammalian liver and excretion of beta aminoisobutyrate by man journal J. Biol. Chem. volume 244 pages 335&ndash 40 pmid 5773299 issue 2 cite journal author Tamaki N, Sakata SF, Matsuda K year 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 Category EC 2.6.1 Category Enzymes of unknown structure transferase stub ... more details
enzyme Name aspartate phenylpyruvate transaminase EC number 2.6.1.70 CAS number 99533 45 6 IUBMB EC number 2 6 1 70 GO code 0047319 image width caption In enzymology , an aspartate phenylpyruvate transaminase EC number 2.6.1.70 is an enzyme that catalysis catalyzes the chemical reaction L aspartate phenylpyruvate math rightleftharpoons math oxaloacetate L phenylalanine Thus, the two substrate biochemistry substrates of this enzyme are L aspartate and phenylpyruvate , whereas its two product chemistry products are oxaloacetate and L phenylalanine . 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 aspartate phenylpyruvate aminotransferase . This enzyme is also called aspartate phenylpyruvate aminotransferase . References reflist 1 cite journal author Holger Z and Kula M R date 1985 title Isolation and characterization of a highly inducible L aspartate phenylpyruvate transaminase from Pseudomonas putida journal J. Biotechnol. volume 3 pages 19&ndash 31 doi 10.1016 0168 1656 85 90004 5 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name cephalosporin C transaminase EC number 2.6.1.74 CAS number 122096 91 7 IUBMB EC number 2 6 1 74 GO code 0047740 image width caption In enzymology , a cephalosporin C transaminase EC number 2.6.1.74 is an enzyme that catalysis catalyzes the chemical reaction 7R 7 5 carboxy 5 oxopentanoyl aminocephalosporinate D glutamate math rightleftharpoons math cephalosporin C 2 oxoglutarate Thus, the two substrate biochemistry substrates of this enzyme are 7R 7 5 carboxy 5 oxopentanoyl aminocephalosporinate and D glutamate , whereas its two product chemistry products are cephalosporin C and 2 oxoglutarate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is cephalosporin C 2 oxoglutarate aminotransferase . Other names in common use include cephalosporin C aminotransferase , and L alanine cephalosporin C aminotransferase . This enzyme participates in penicillin and cephalosporin biosynthesis . References reflist 1 cite journal author Aretz W, Sauber K date 1988 title Novel D amino acid transaminase journal Ann. N. Y. Acad. Sci. volume 542 pages 366 70 pmid 3228235 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name cysteine conjugate transaminase EC number 2.6.1.75 CAS number 117698 05 2 IUBMB EC number 2 6 1 75 GO code 0047802 image width caption In enzymology , a cysteine conjugate transaminase EC number 2.6.1.75 is an enzyme that catalysis catalyzes the chemical reaction S 4 bromophenyl L cysteine 2 oxoglutarate math rightleftharpoons math S 4 bromophenyl mercaptopyruvate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are S 4 bromophenyl L cysteine and 2 oxoglutarate , whereas its two product chemistry products are S 4 bromophenyl 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 S 4 bromophenyl L cysteine 2 oxoglutarate aminotransferase . Other names in common use include cysteine conjugate aminotransferase , and cysteine conjugate alpha ketoglutarate transaminase CAT 1 . References reflist 1 cite journal author Tateishi M date 1988 title Purification and characterization of cysteine conjugate transaminases from rat liver journal Xenobiotica volume 18 pages 1015&ndash 28 pmid 2852419 doi 10.3109 00498258809042224 last2 Ichimoto first2 N last3 Takanohashi first3 Y last4 Ichihara first4 S last5 Fukazawa first5 H last6 Tateishi first6 M issue 9 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name diaminobutyrate pyruvate transaminase EC number 2.6.1.46 CAS number 37277 95 5 IUBMB EC number 2 6 1 46 GO code 0047307 image width caption In enzymology , a diaminobutyrate pyruvate transaminase EC number 2.6.1.46 is an enzyme that catalysis catalyzes the chemical reaction L 2,4 diaminobutanoate pyruvate math rightleftharpoons math L aspartate 4 semialdehyde L alanine Thus, the two substrate biochemistry substrates of this enzyme are L 2,4 diaminobutanoate and pyruvate , whereas its two product chemistry products are L aspartate 4 semialdehyde 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 L 2,4 diaminobutanoate pyruvate aminotransferase . Other names in common use include diaminobutyrate pyruvate aminotransferase , and L diaminobutyric acid transaminase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Rao DR, Hariharan K, Vijayalakshmi KR date 1969 title A study of the metabolism of L alpha gamma diaminobutyric acid in a Xanthomonas species journal Biochem. J. volume 114 pages 107&ndash 15 pmid 4390206 issue 1 pmc 1184802 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name D methionine pyruvate transaminase EC number 2.6.1.41 CAS number 37277 93 3 IUBMB EC number 2 6 1 41 GO code 0047306 image width caption In enzymology , a D methionine pyruvate transaminase EC number 2.6.1.41 is an enzyme that catalysis catalyzes the chemical reaction D methionine pyruvate math rightleftharpoons math 4 methylthio 2 oxobutanoate L alanine Thus, the two substrate biochemistry substrates of this enzyme are D methionine and pyruvate , whereas its two product chemistry products are 4 methylthio 2 oxobutanoate 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 D methionine pyruvate aminotransferase . Other names in common use include D methionine transaminase , and D methionine aminotransferase . This enzyme participates in d alanine metabolism . References reflist 1 cite journal author Mapson LW, March JF, Wardale DA date 1969 title Biosynthesis of ethylene. 4 methylmercapto 2 oxobutyric acid an intermediate in the formation from methionine journal Biochem. J. volume 115 pages 653&ndash 61 pmid 5357015 issue 4 pmc 1185190 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name pyridoxamine oxaloacetate transaminase EC number 2.6.1.31 CAS number 37277 88 6 IUBMB EC number 2 6 1 31 GO code 0019162 image width caption In enzymology , a pyridoxamine oxaloacetate transaminase EC number 2.6.1.31 is an enzyme that catalysis catalyzes the chemical reaction pyridoxamine oxaloacetate math rightleftharpoons math pyridoxal L aspartate Thus, the two substrate biochemistry substrates of this enzyme are pyridoxamine and oxaloacetate , whereas its two product chemistry products are pyridoxal and L aspartate . This enzyme belongs to the family of transferase s, specifically the transaminases , which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine oxaloacetate aminotransferase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . References reflist 1 cite journal author Wada H and Snell EE date 1962 title Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha ketoglutarate journal J. Biol. Chem. volume 237 pages 127&ndash 132 pmid 14004226 cite journal author Wu, HLC and Mason M date 1964 title Pyridoxamine oxaloacetic transaminase of rat kidney journal J. Biol. Chem. volume 239 pages 1492&ndash 1497 pmid 14189882 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name Thyroid hormone transaminase EC number 2.6.1.26 CAS number 51004 29 6 IUBMB EC number 2 6 1 26 GO code image width caption In enzymology , a thyroid hormone transaminase EC number 2.6.1.26 is an enzyme that catalysis catalyzes the chemical reaction L 3,5,3 triiodothyronine 2 oxoglutarate math rightleftharpoons math 3 4 4 hydroxy 3 iodophenoxy 3,5 diiodophenyl 2 oxopropanoate L glutamate Thus, the two substrate biochemistry substrates of this enzyme are L 3,5,3 triiodothyronine and 2 oxoglutarate , whereas its two product chemistry products are 3 4 4 hydroxy 3 iodophenoxy 3,5 diiodophenyl 2 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 L 3,5,3 triiodothyronine 2 oxoglutarate aminotransferase . Other names in common use include 3,5 dinitrotyrosine transaminase , and thyroid hormone aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Soffer RL, Hechtman P, Savage M date 1973 title L Triiodothyronine aminotransferase journal J. Biol. Chem. volume 248 pages 1224&ndash 30 pmid 4686924 issue 4 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name taurine 2 oxoglutarate transaminase EC number 2.6.1.55 CAS number 9076 52 2 IUBMB EC number 2 6 1 55 GO code 0050322 image width caption In enzymology , a taurine 2 oxoglutarate transaminase EC number 2.6.1.55 is an enzyme that catalysis catalyzes the chemical reaction taurine 2 oxoglutarate math rightleftharpoons math sulfoacetaldehyde L glutamate Thus, the two substrate biochemistry substrates of this enzyme are taurine and 2 oxoglutarate , whereas its two product chemistry products are sulfoacetaldehyde 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 taurine 2 oxoglutarate aminotransferase . Other names in common use include taurine aminotransferase , taurine transaminase , taurine alpha ketoglutarate aminotransferase , and taurine glutamate transaminase . This enzyme participates in beta alanine metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Toyama S, Misono H, Soda K date 1972 title Crystalline taurine ketoglutarate aminotransferase from Achromobacter superficialis journal Biochem. Biophys. Res. Commun. volume 46 pages 1374&ndash 9 pmid 5012173 doi 10.1016 S0006 291X 72 80127 X issue 3 cite journal author Cook AM, Denger K date 2002 title Dissimilation of the C2 sulfonates journal Arch. Microbiol. volume 179 pages 1&ndash 6 pmid 12471498 doi 10.1007 s00203 002 0497 0 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name glycine oxaloacetate transaminase EC number 2.6.1.35 CAS number 37277 90 0 IUBMB EC number 2 6 1 35 GO code 0047303 image width caption In enzymology , a glycine oxaloacetate transaminase EC number 2.6.1.35 is an enzyme that catalysis catalyzes the chemical reaction glycine oxaloacetate math rightleftharpoons math glyoxylate L aspartate Thus, the two substrate biochemistry substrates of this enzyme are glycine and oxaloacetate , whereas its two product chemistry products are glyoxylate and L aspartate . 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 oxaloacetate aminotransferase . This enzyme is also called glycine oxaloacetate aminotransferase . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author Gibbs RG and Morris JG date 1966 title Formation of glycine from glyoxylate in Micrococcus denitrificans journal Biochem. J. volume 99 pages 27 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
enzyme Name kynurenine glyoxylate transaminase EC number 2.6.1.63 CAS number 74506 33 5 IUBMB EC number 2 6 1 63 GO code 0047315 image width caption In enzymology , a kynurenine glyoxylate transaminase EC number 2.6.1.63 is an enzyme that catalysis catalyzes the chemical reaction L kynurenine glyoxylate math rightleftharpoons math 4 2 aminophenyl 2,4 dioxobutanoate glycine Thus, the two substrate biochemistry substrates of this enzyme are L kynurenine and glyoxylate , whereas its two product chemistry products are 4 2 aminophenyl 2,4 dioxobutanoate and glycine . 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 kynurenine glyoxylate aminotransferase cyclizing . This enzyme is also called kynurenine glyoxylate aminotransferase . References reflist 1 cite journal author Harada I date 1980 title Glucagen inducible kynurenine aminotransferase. journal Wakayama Igaku volume 31 pages 61&ndash 68 transferase stub Category EC 2.6.1 Category Enzymes of unknown structure ... more details
enzyme Name 2 aminoethylphosphonate pyruvate transaminase EC number 2.6.1.37 CAS number 37277 91 1 IUBMB EC number 2 6 1 37 GO code 0047304 image width caption orphan date December 2008 In enzymology , a 2 aminoethylphosphonate pyruvate transaminase EC number 2.6.1.37 is an enzyme that catalysis catalyzes the chemical reaction 2 aminoethyl phosphonate pyruvate math rightleftharpoons math 2 phosphonoacetaldehyde L alanine Thus, the two substrate biochemistry substrates of this enzyme are 2 aminoethyl phosphonate and pyruvate , whereas its two product chemistry products are 2 phosphonoacetaldehyde 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 2 aminoethyl phosphonate pyruvate aminotransferase . Other names in common use include 2 aminoethyl phosphonate transaminase , 2 aminoethyl phosphonate aminotransferase , 2 aminoethyl phosphonic acid aminotransferase , 2 aminoethylphosphonate pyruvate aminotransferase , 2 aminoethylphosphonate aminotransferase , 2 aminoethylphosphonate transaminase , AEP transaminase , and AEPT . This enzyme participates in aminophosphonate metabolism . 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 1M32 . References reflist 1 cite journal author La Nauze JM, Rosenberg H date 1968 title The identification of 2 phosphonoacetaldehyde as an intermediate in the degradation of 2 aminoethylphosphonate by Bacillus cereus journal Biochim. Biophys. Acta. volume 165 pages 438&ndash 47 pmid 4982500 issue 3 cite journal author Dumora C, Lacoste AM, Cassaigne A date 1983 title Purification and properties of 2 aminoethylphosphonate pyruvate aminotransferase from Pseudomonas aeruginosa journal Eur. J. Biochem. volume 133 pages 119&ndash 25 ... more details
enzyme Name adenosylmethionine 8 amino 7 oxononanoate transaminase EC number 2.6.1.62 CAS number 37259 71 5 IUBMB EC number 2 6 1 62 GO code 0004015 image width caption In enzymology , an adenosylmethionine 8 amino 7 oxononanoate transaminase EC number 2.6.1.62 is an enzyme that catalysis catalyzes the chemical reaction S adenosyl L methionine 8 amino 7 oxononanoate math rightleftharpoons math S adenosyl 4 methylthio 2 oxobutanoate 7,8 diaminononanoate Thus, the two substrate biochemistry substrates of this enzyme are S adenosyl L methionine and 8 amino 7 oxononanoate , whereas its two product chemistry products are S adenosyl 4 methylthio 2 oxobutanoate and 7,8 diaminononanoate . 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 adenosyl L methionine 8 amino 7 oxononanoate aminotransferase . Other names in common use include 7,8 diaminonanoate transaminase , 7,8 diaminononanoate transaminase , DAPA transaminase , 7,8 diaminopelargonic acid aminotransferase , DAPA aminotransferase , 7 keto 8 aminopelargonic acid , diaminopelargonate synthase , and 7 keto 8 aminopelargonic acid aminotransferase . This enzyme participates in biotin metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . Structural studies As of late 2007, 11 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1DTY , PDB link 1MGV , PDB link 1MLY , PDB link 1MLZ , PDB link 1QJ3 , PDB link 1QJ5 , PDB link 1S06 , PDB link 1S07 , PDB link 1S08 , PDB link 1S09 , and PDB link 1S0A . References reflist 1 cite journal author Izumi Y, Sato K, Tani Y and Ogata K date 1973 title Purification of 7 keto 8 aminopelargonic acid 7,8 diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis, from Brevibacterium divaricatum journal Agric. Biol. Chem. volume 37 pages 2683&ndash 2684 cite ... more details
enzyme Name beta alanine pyruvate transaminase EC number 2.6.1.18 CAS number 9030 47 1 IUBMB EC number 2 6 1 18 GO code 0016223 image width caption In enzymology , a beta alanine pyruvate transaminase EC number 2.6.1.18 is an enzyme that catalysis catalyzes the chemical reaction L alanine 3 oxopropanoate math rightleftharpoons math pyruvate beta alanine Thus, the two substrate biochemistry substrates of this enzyme are L alanine and 3 oxopropanoate , whereas its two product chemistry products are pyruvate and beta 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 L alanine 3 oxopropanoate aminotransferase . Other names in common use include beta alanine pyruvate aminotransferase , and beta alanine alpha alanine transaminase . This enzyme participates in 4 metabolism metabolic pathways alanine and aspartate metabolism , valine, leucine and isoleucine degradation , beta alanine metabolism , and propanoate metabolism . It employs one cofactor biochemistry cofactor , pyridoxal phosphate . References reflist 1 cite journal author HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S date 1961 title Enzymatic studies on the metabolism of beta alanine journal J. Biol. Chem. volume 236 pages 781&ndash 90 pmid 13712439 cite journal author Stinson RA, Spencer MS date 1969 title Beta alanine aminotransferase s from a plant source journal Biochem. Biophys. Res. Commun. volume 34 pages 120&ndash 7 pmid 5762452 doi 10.1016 0006 291X 69 90537 3 issue 1 transferase stub Category EC 2.6.1 Category Pyridoxal phosphate enzymes Category Enzymes of unknown structure ... more details
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