Accepted name: serine—pyruvate transaminase
Reaction: L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
For diagram click here (mechanism).
Other name(s): SPT; hydroxypyruvate:L-alanine transaminase
Systematic name: L-serine:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. The liver enzyme may be identical with EC 2.6.1.44 alanine-glyoxylate transaminase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9030-88-0
References:
1. Cheung, G.P., Rosenblum, I. and Sallach, H.J. Comparative studies of enzymes related to serine metabolism in higher plants. Plant Physiol. 43 (1968) 1813-1820. [PMID: 5699148]
2. Kretovich, V.L. and Stepanovich, K.M. [The synthesis of serine from hydroxypyruvate in plants.] Dokl. Akad. Nauk S.S.S.R. 139 (1961) 488-490. (in Russian)
3. Sallach, H.J. Formation of serine from hydroxypyruvate and L-alanine. J. Biol. Chem. 223 (1956) 1101-1108.
Accepted name: phosphoserine transaminase
Reaction: (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate
(2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
For diagram, click here or here or here for mechanism click here.
Other name(s): PSAT; phosphoserine aminotransferase; 3-phosphoserine aminotransferase; hydroxypyruvic phosphate-glutamic transaminase; L-phosphoserine aminotransferase; phosphohydroxypyruvate transaminase; phosphohydroxypyruvic-glutamic transaminase; phosphoserine aminotransferase; 3-O-phospho-L-serine:2-oxoglutarate aminotransferase; SerC; PdxC; 3PHP transaminase
Systematic name: O-phospho-L-serine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli [2,3]. It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in Escherichia coli (using Reaction 2 above) [3]. In Escherichia coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9030-90-4
References:
1. Hirsch, H. and Greenberg, D.M. Studies on phosphoserine aminotransferase of sheep brain. J. Biol. Chem. 242 (1967) 2283-2287. [PMID: 6022873]
2. Pizer, L.I. The pathway and control of serine biosynthesis in Escherichia coli. J. Biol. Chem. 238 (1963) 3934-3944. [PMID: 14086727]
3. Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232-239. [PMID: 8550422]
4. Drewke, C., Klein, M., Clade, D., Arenz, A., Müller, R. and Leistner, E. 4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis. FEBS Lett. 390 (1996) 179-182. [PMID: 8706854]
5. Zhao, G. and Winkler, M.E. 4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12. FEMS Microbiol. Lett. 135 (1996) 275-280. [PMID: 8595869]
[EC 2.6.1.53 Transferred entry: now EC 1.4.1.13 glutamate synthase (NADPH2) (EC 2.6.1.53 created 1972, deleted 1976)]
Accepted name: pyridoxamine-phosphate transaminase
Reaction: pyridoxamine 5'-phosphate + 2-oxoglutarate = pyridoxal 5'-phosphate + D-glutamate
Other name(s): pyridoxamine phosphate aminotransferase; pyridoxamine 5'-phosphate-α-ketoglutarate transaminase; pyridoxamine 5'-phosphate transaminase
Systematic name: pyridoxamine-5'-phosphate:2-oxoglutarate aminotransferase (D-glutamate-forming)
Comments: Also acts, more slowly, on pyridoxamine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9074-84-4
References:
1. Tani, Y., Ukita, M. and Ogata, K. Studies on vitamin B6 metabolism in microorganisms. Part X. Further purification and characterization of pyridoxamine 5'-phosphate-α-ketoglutarate transaminase from Clostridium kainantoi. Agric. Biol. Chem. 36 (1972) 181-188.
Accepted name: taurine—2-oxoglutarate transaminase
Reaction: taurine + 2-oxoglutarate = 2-sulfoacetaldehyde + L-glutamate
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): taurine aminotransferase; taurine transaminase; taurine—α-ketoglutarate aminotransferase; taurine—glutamate transaminase
Systematic name: taurine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on D,L-3-amino-isobutanoate, β-alanine and 3-aminopropanesulfonate. Involved in the microbial utilization of β-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 9076-52-2
References:
1. Toyama, S., Misono, H. and Soda, K. Crystalline taurine:α-ketoglutarate aminotransferase from Achromobacter superficialis. Biochem. Biophys. Res. Commun. 46 (1972) 1374-1379. [PMID: 5012173]
2. Cook, A.M. and Denger, K. Dissimilation of the C2 sulfonates. Arch. Microbiol. 179 (2002) 1-6. [PMID: 12471498]
Accepted name: 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase
Reaction: 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol + pyruvate = 1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol + L-alanine
Other name(s): guanidinoaminodideoxy-scyllo-inositol-pyruvate aminotransferase; L-alanine-N-amidino-3-(or 5-)keto-scyllo-inosamine transaminase
Systematic name: 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol:pyruvate aminotransferase
Comments: L-Glutamate and L-glutamine can also act as amino donors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 57127-19-2
References:
1. Walker, J.B. Enzymatic reactions involved in streptomycin biosynthesis and metabolism. Lloydia 34 (1971) 363-371.
2. Walker, J.B. and Walker, M.S. Streptomycin biosynthesis. Transamination reactions involving inosamines and inosadiamines. Biochemistry 8 (1969) 763-770. [PMID: 5781017]
Accepted name: aromatic-amino-acid transaminase
Reaction: An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate
For diagram click here or here.
Other name(s): aromatic amino acid aminotransferase; aromatic aminotransferase; ArAT
Systematic name: aromatic-amino-acid:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Methionine can also act as donor, but more slowly; oxaloacetate can act as acceptor. Controlled proteolysis converts the enzyme into EC 2.6.1.1 aspartate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37332-38-0
References:
1. Mavrides, C. and Orr, W. Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli. J. Biol. Chem. 250 (1975) 4128-4133. [PMID: 236311]
Accepted name: phenylalanine(histidine) transaminase
Reaction: L-phenylalanine + pyruvate = phenylpyruvate + L-alanine
For diagram click here (mechanism).
Other name(s): phenylalanine (histidine) aminotransferase; phenylalanine(histidine):pyruvate aminotransferase; histidine:pyruvate aminotransferase; L-phenylalanine(L-histidine):pyruvate aminotransferase
Systematic name: L-phenylalanine:pyruvate aminotransferase
Comments: L-Histidine and L-tyrosine can act instead of L-phenylalanine; in the reverse reaction, L-methionine, L-serine and L-glutamine can replace L-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 72560-98-6
References:
1. Minatogawa, Y., Noguchi, T. and Kido, R. Species distribution and properties of hepatic phenylalanine (histidine):pyruvate aminotransferase. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 59-67. [PMID: 14070]
Accepted name: dTDP-4-amino-4,6-dideoxygalactose transaminase
Reaction: dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-D-galactose + L-glutamate
Glossary: dTDP-4-dehydro-6-deoxy-D-galactose = dTDP-4-dehydro-6-deoxy-D-glucose
Other name(s): thymidine diphosphoaminodideoxygalactose aminotransferase; thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase; WecE
Systematic name: dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 72560-97-5
References:
1. Ohashi, H., Matsuhashi, M. and Matsuhashi, S. Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. IV. Purification and properties of thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase from Pasteurella pseudotuberculosis. J. Biol. Chem. 246 (1971) 2325-2330. [PMID: 4928644]
2. Hwang, B.Y., Lee, H.J., Yang, Y.H., Joo, H.S. and Kim, B.G. Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12. Chem. Biol. 11 (2004) 915–925. [PMID: 15271350]
Accepted name: aromatic-amino-acid—glyoxylate transaminase
Reaction: an aromatic amino acid + glyoxylate = an aromatic oxo acid + glycine
Systematic name: aromatic-amino-acid:glyoxylate aminotransferase
Comments: Phenylalanine, kynurenine, tyrosine and histidine can act as amino donors; glyoxylate, pyruvate and hydroxypyruvate can act as amino acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 67185-76-6
References:
1. Harada, I., Noguchi, T. and Kido, R. Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver. Hoppe-Seyler's Z. Physiol. Chem. 359 (1978) 481-488. [PMID: 25837]
[EC 2.6.1.61 Deleted entry: (R)-3-amino-2-methylpropionate transaminase. Enzyme is identical to EC 2.6.1.40, (R)-3-amino-2-methylpropionate—pyruvate transaminase (EC 2.6.1.61 created 1982, deleted 2004)]
Accepted name: adenosylmethionine—8-amino-7-oxononanoate transaminase
Reaction: S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Other name(s): 7,8-diaminonanoate transaminase; 7,8-diaminononanoate transaminase; DAPA transaminase; 7,8-diaminopelargonic acid aminotransferase; DAPA aminotransferase; 7-keto-8-aminopelargonic acid; diaminopelargonate synthase; 7-keto-8-aminopelargonic acid aminotransferase
Systematic name: S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase
Comments: S-adenosylhomocysteine can also act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, PDB, CAS registry number: 37259-71-5
References:
1. Izumi, Y., Sato, K., Tani, Y. and Ogata, K. Purification of 7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis, from Brevibacterium divaricatum. Agric. Biol. Chem. 37 (1973) 2683-2684.
2. Izumi, Y., Sato, K., Tani, Y. and Ogata, K. 7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis by microorganisms. Agric. Biol. Chem. 39 (1975) 175-181.
3. Stoner, G.L. and Eisenberg, M.A. Purification and properties of 7,8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway. J. Biol. Chem. 250 (1973) 4029-4036.
Accepted name: kynurenine—glyoxylate transaminase
Reaction: L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
For diagram click here (mechanism).
Other name(s): kynurenine-glyoxylate aminotransferase
Systematic name: L-kynurenine:glyoxylate aminotransferase (cyclizing)
Comments: Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 74506-33-5
References:
1. Harada, I. [Glucagen inducible kynurenine aminotransferase.] Wakayama Igaku 31 (1980) 61-68. (in Japanese)
Accepted name: glutamine—phenylpyruvate transaminase
Reaction: L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine
For diagram click here (mechanism).
Other name(s): glutamine transaminase K; glutamine-phenylpyruvate aminotransferase
Systematic name: L-glutamine:phenylpyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Methionine, L-histidine and L-tyrosine can act as donors. The enzyme has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15 glutamine—pyruvate transaminase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 68518-06-9
References:
1. Cooper, A.J.L. Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L-phenylalanine and α-keto-γ-methiolbutyrate. Anal. Biochem. 89 (1978) 451-460. [PMID: 727444]
2. Cooper, A.J.L. and Meister, A. Isolation and properties of a new glutamine transaminase from rat kidney. J. Biol. Chem. 249 (1974) 2554-2561. [PMID: 4822504]
Accepted name: N6-acetyl-β-lysine transaminase
Reaction: 6-acetamido-3-aminohexanoate + 2-oxoglutarate = 6-acetamido-3-oxohexanoate + L-glutamate
Other name(s): ε-acetyl-β-lysine aminotransferase
Systematic name: 6-acetamido-3-aminohexanoate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 71768-10-0
References:
1. Bozler, G., Robertson, J.M., Ohsugi, M., Hensley, C. and Barker, H.A. Metabolism of L-β-lysine in a Pseudomonas: conversion of 6-N-acetyl-L-β-lysine to 3-keto-6-acetamidohexanoate and of 4-aminobutyrate to succinic semialdehyde by different transaminases. Arch. Biochem. Biophys. 197 (1979) 226-235. [PMID: 44448]
Accepted name: valine—pyruvate transaminase
Reaction: L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine
For diagram click here and another example (mechanism).
Other name(s): transaminase C; valine-pyruvate aminotransferase; alanine-oxoisovalerate aminotransferase
Systematic name: L-valine:pyruvate aminotransferase
Comments: Different from EC 2.6.1.42, branched-chain-amino-acid-transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 73379-50-7
References:
1. Falkinham, J.O., III Identification of a mutation affecting an alanine-α-ketoisovalerate transaminase activity in Escherichia coli K-12. Mol. Gen. Genet. 176 (1979) 147-149. [PMID: 396446]
2. Rudman, D. and Meister, A. Transamination in Escherichia coli. J. Biol. Chem. 200 (1953) 591-604.
Accepted name: 2-aminohexanoate transaminase
Reaction: L-2-aminohexanoate + 2-oxoglutarate = 2-oxohexanoate + L-glutamate
For diagram click here (mechanism).
Other name(s): norleucine transaminase; norleucine (leucine) aminotransferase; leucine L-norleucine: 2-oxoglutarate aminotransferase
Systematic name: L-2-aminohexanoate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on L-leucine and, more slowly, on L-isoleucine, L-2-aminopentanoate and L-aspartate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 111310-35-1
References:
1. Der Garabedian, P.A. and Vermeersch, J.J. Candida L-norleucine, leucine:2-oxoglutarate aminotransferase. Purification and properties. Eur. J. Biochem. 167 (1987) 141-147. [PMID: 3622507]
Accepted name: ornithine(lysine) transaminase
Reaction: L-ornithine + 2-oxoglutarate = 3,4-dihydro-2H-pyrrole-2-carboxylate + L-glutamate + H2O
Other name(s): ornithine(lysine) aminotransferase; lysine/ornithine:2-oxoglutarate aminotransferase; L-ornithine(L-lysine):2-oxoglutarate-aminotransferase
Systematic name: L-ornithine:2-oxoglutarate-aminotransferase
Comments: The enzyme from Trichomonas vaginalis also acts on L-lysine, producing 2,3,4,5-tetrahydropyridine-2-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 105542-39-0
References:
1. Lowe, P.N. and Rowe, A.F. Aminotransferase activities in Trichomonas vaginalis. Mol. Biochem. Parasitol. 21 (1986) 65-74. [PMID: 3095639]
[EC 2.6.1.69 Deleted entry: N2-acetylornithine 5-transaminase. Enzyme is identical to EC 2.6.1.11, acetylornithine transaminase (EC 2.6.1.69 created 1989, deleted 2004)]
Accepted name: aspartate—phenylpyruvate transaminase
Reaction: L-aspartate + phenylpyruvate = oxaloacetate + L-phenylalanine
For diagram click here (mechanism).
Other name(s): aspartate-phenylpyruvate aminotransferase
Systematic name: L-aspartate:phenylpyruvate aminotransferase
Comments: The enzyme from Pseudomonas putida also acts on 4-hydroxy-phenylpyruvate and, more slowly, on L-glutamate and L-histidine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 99533-45-6
References:
1. Holger, Z. and Kula, M.-R. Isolation and characterization of a highly inducible L-aspartate-phenylpyruvate transaminase from Pseudomonas putida. J. Biotechnol. 3 (1985) 19-31.
Accepted name: lysine—pyruvate 6-transaminase
Reaction: L-lysine + pyruvate = (S)-2-amino-6-oxohexanoate + L-alanine
For diagram click here.
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): lysine-pyruvate aminotransferase; Lys-AT
Systematic name: L-lysine:pyruvate aminotransferase
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 114189-79-6
References:
1. Schmidt, H., Bode, R. and Birnbaum, D. A novel enzyme, L-lysine : pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii. FEMS Microbiol. Lett. 49 (1988) 203-206.
Accepted name: D-4-hydroxyphenylglycine transaminase
Reaction: D-4-hydroxyphenylglycine + 2-oxoglutarate = 4-hydroxyphenylglyoxylate + L-glutamate
Other name(s): D-hydroxyphenylglycine aminotransferase
Systematic name: D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 117444-05-0
References:
1. Van den Tweel, W.J.J., Ogg, R.L.H.P. and de Bont, J.A.M. Transamination with a D-transaminase from Pseudomonas putida and conversion of p-hydroxyphenylglyoxylate to D-p-hydroxyphenylglycine. Neth. Appl. NL 87 (1987) 02449, 14 Oct. 1987.
2. Van den Tweel, W.J.J., Smits, J.P., Ogg, R.L.H.P. and de Bont, J.A.M. The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine in Pseudomonas putida. Appl. Microbiol. Biotechnol. 29 (1988) 224-230.
Accepted name: methionine—glyoxylate transaminase
Reaction: L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine
For diagram click here (mechanism).
Other name(s): methionine-glyoxylate aminotransferase; MGAT
Systematic name: L-methionine:glyoxylate aminotransferase
Comments: L-Glutamate can also act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 116155-75-0
References:
1. Glover, J.R., Chapple, C.C.S., Rothwell, S., Tober, I. and Ellis, B.E. Allylglucosinolate biosynthesis in Brassica carinata. Phytochemistry 27 (1988) 1345-1348.
Accepted name: cephalosporin-C transaminase
Reaction: (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate + D-glutamate = cephalosporin C + 2-oxoglutarate
For diagram click here.
Glossary: cephalosporin C = (7R)-7-(5-carboxy-5-oxopentanamido)cephalosporanate
Other name(s): cephalosporin C aminotransferase; L-alanine:cephalosporin-C aminotransferase
Systematic name: cephalosporin-C:2-oxoglutarate aminotransferase
Comments: A number of D-amino acids, including D-alanine, D-aspartate and D-methionine can also act as amino-group donors. Although this enzyme acts on several free D-amino acids, it differs from EC 2.6.1.21, D-alanine transaminase, in that it can use cephalosporin C as an amino donor.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 122096-91-7
References:
1. Aretz, W. and Sauber, K. Novel D-amino acid transaminase. Ann. N.Y. Acad. Sci. 542 (1988) 366-370. [PMID: 3228235]
Accepted name: cysteine-conjugate transaminase
Reaction: S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate = S-(4-bromophenyl)mercaptopyruvate + L-glutamate
For diagram click here (mechanism).
Other name(s): cysteine conjugate aminotransferase; cysteine-conjugate α-ketoglutarate transaminase (CAT-1)
Systematic name: S-(4-bromophenyl)-L-cysteine:2-oxoglutarate aminotransferase
Comments: A number of cysteine conjugates can also act.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 117698-05-2
References:
1. Tomisawa, H., Ichimoto, N., Takanohashi, Y., Ichihara, S., Fukazawa, H. and Tateishi, M. Purification and characterization of cysteine conjugate transaminases from rat liver. Xenobiotica 18 (1988) 1015-1028. [PMID: 2852419]
Accepted name: diaminobutyrate—2-oxoglutarate transaminase
Reaction: L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate
For diagram, click here
Other name(s): L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase; 2,4-diaminobutyrate 4-aminotransferase; diaminobutyrate aminotransferase; DABA aminotransferase; DAB aminotransferase; EctB; diaminibutyric acid aminotransferase; L-2,4-diaminobutyrate:2-oxoglutarate 4-aminotransferase
Systematic name: L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase
Comments: A pyridoxal-phosphate protein that requires potassium for activity [4]. In the proteobacterium Acinetobacter baumannii, this enzyme is cotranscribed with the neighbouring ddc gene that also encodes EC 4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46, diaminobutyrate—pyruvate transaminase, which has pyruvate as the amino-group acceptor. This is the first enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108, ectoine synthase [3,4].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 196622-96-5
References:
1. Ikai, H. and Yamamoto, S. Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii. J. Bacteriol. 179 (1997) 5118-5125. [PMID: 9260954]
2. Ikai, H. and Yamamoto, S. Two genes involved in the 1,3-diaminopropane production pathway in Haemophilus influenzae. Biol. Pharm. Bull. 21 (1998) 170-173. [PMID: 9514614]
3. Peters, P., Galinski, E.A. and Truper, H.G. The biosynthesis of ectoine. FEMS Microbiol. Lett. 71 (1990) 157-162.
4. Ono, H., Sawada, K., Khunajakr, N., Tao, T., Yamamoto, M., Hiramoto, M., Shinmyo, A., Takano, M. and Murooka, Y. Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata. J. Bacteriol. 181 (1999) 91-99. [PMID: 9864317]
5. Kuhlmann, A.U. and Bremer, E. Osmotically regulated synthesis of the compatible solute ectoine in Bacillus pasteurii and related Bacillus spp. Appl. Environ. Microbiol. 68 (2002) 772-783. [PMID: 11823218]
6. Louis, P. and Galinski, E.A. Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli. Microbiology 143 (1997) 1141-1149. [PMID: 9141677]
Accepted name: taurine—pyruvate aminotransferase
Reaction: taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde
For diagram click here.
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): Tpa
Systematic name: taurine:pyruvate aminotransferase
Comments: The enzyme from Bilophila wadsworthia requires pryidoxal 5'-phosphate as a cofactor, is reversible, and catalyses the first step of anaerobic taurine degradation. Hypotaurine (i.e. 2-aminoethanesulfinate) and β-alanine are also significant donors of an amino group. Unlike, EC 2.6.1.55, taurine—2-oxoglutarate transaminase, 2-oxoglutarate is not an acceptor of amino groups.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 51901-18-9
References:
1. Laue, H. and Cook, A.M. Biochemical and molecular characterization of taurine:pyruvate transaminase from the anaerobe Bilophila wadsworthia. Eur. J. Biochem. 267 (2000) 6841-6848. [PMID: 11082195]
2. Cook, A.M. and Denger, K. Dissimilation of the C2 sulfonates. Arch. Microbiol. 179 (2002) 1-6. [PMID: 12471498]
3. Masepohl, B., Fuhrer, F. and Klipp, W. Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source. FEMS Microbiol. Lett. 205 (2001) 105-111. [PMID: 11728723]
Accepted name: aspartate—prephenate aminotransferase
Reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate
For diagram click here.
Other name(s): prephenate transaminase (ambiguous); PAT (ambiguous); prephenate aspartate aminotransferase; L-aspartate:prephenate aminotransferase
Systematic name: L-arogenate:oxaloacetate aminotransferase
Comments: A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate—prephenate aminotransferase).
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. De-Eknamkul, W. and Ellis, B.E. Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures. Arch. Biochem. Biophys. 267 (1988) 87-94. [PMID: 3196038]
Accepted name: glutamate—prephenate aminotransferase
Reaction: L-arogenate + 2-oxoglutarate = prephenate + L-glutamate
For diagram click here.
Other name(s): prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase
Systematic name: L-arogenate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate—prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate [1].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Bonner, C.A. and Jensen, R.A. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 238 (1985) 237-246. [PMID: 3985619]
2. Siehl, D.L., Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase. Z. Naturforsch. [C] 41 (1986) 79-86. [PMID: 2939644]
3. Bonner, C. and Jensen, R. Prephenate aminotransferase. Methods Enzymol. 142 (1987) 479-487. [PMID: 3298985]
Accepted name: nicotianamine aminotransferase
Reaction: nicotianamine + 2-oxoglutarate = 3"-deamino-3"-oxonicotianamine + L-glutamate
For diagram click here.
Other name(s): NAAT; NAAT-I; NAAT-II; NAAT-III; nicotianamine transaminase
Systematic name: nicotianamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. This enzyme is produced by grasses. They secrete both the nicotianamine and the transaminated product into the soil around them. Both compounds chelate iron(II) and iron(III); these chelators, called mugineic acid family phytosiderophores, are taken up by the grass, which is thereby supplied with iron.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 154907-64-9
References:
1. Kanazawa, K., Higuchi, K., Nishizawa, N.-K., Fushiya, S., Chino, M. and Mori, S. Nicotianamine aminotransferase activities are correlated with the phytosiderophore secretions under Fe-deficient conditions in Gramineae. J. Exp. Bot. 45 (1994) 1903-1906.
2. Takahashi, M., Yamaguchi, H., Nakanishi, H., Shioiri, T., Nishizawa, N.K. and Mori, S. Cloning two genes for nicotianamine aminotransferase, a critical enzyme in iron acquisition (Strategy II) in graminaceous plants. Plant Physiol. 121 (1999) 947-956. [PMID: 10557244]
3. Schaaf, G., Ludewig, U., Erenoglu, B.E., Mori, S., Kitahara, T. and von Wirén, N. ZmYS1 functions as a proton-coupled symporter for phytosideorophore- and nicotianamine-chelated metals. J. Biol. Chem. 279 (2004) 9091-9096. [PMID: 14699112]
Accepted name: succinylornithine transaminase
Reaction: N2-succinyl-L-ornithine + 2-oxoglutarate = N-succinyl-L-glutamate 5-semialdehyde + L-glutamate
For diagram, click here
Other name(s): succinylornithine aminotransferase; N2-succinylornithine 5-aminotransferase; AstC; SOAT
Systematic name: N2-succinyl-L-ornithine:2-oxoglutarate 5-aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on N2-acetyl-L-ornithine and L-ornithine, but more slowly [3]. In Pseudomonas aeruginosa, the arginine-inducible succinylornithine transaminase, acetylornithine transaminase (EC 2.6.1.11) and ornithine aminotransferase (EC 2.6.1.13) activities are catalysed by the same enzyme, but this is not the case in all species [5]. This is the third enzyme in the arginine succinyltransferase (AST) pathway for the catabolism of arginine [1]. This pathway converts the carbon skeleton of arginine into glutamate, with the concomitant production of ammonia and conversion of succinyl-CoA into succinate and CoA. The five enzymes involved in this pathway are EC 2.3.1.109 (arginine N-succinyltransferase), EC 3.5.3.23 (N-succinylarginine dihydrolase), EC 2.6.1.81 (succinylornithine transaminase), EC 1.2.1.71 (succinylglutamate-semialdehyde dehydrogenase) and EC 3.5.1.96 (succinylglutamate desuccinylase) [3, 6]. Of the five enzymes involved in arginine catabolism, this is the only one that is also involved in ornithine catabolism [4].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Vander Wauven, C. and Stalon, V. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. J. Bacteriol. 164 (1985) 882-886. [PMID: 2865249]
2. Schneider, B.L., Kiupakis, A.K. and Reitzer, L.J. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180 (1998) 4278-4286. [PMID: 9696779]
3. Cunin, R., Glansdorff, N., Pierard, A. and Stalon, V. Biosynthesis and metabolism of arginine in bacteria. Microbiol. Rev. 50 (1986) 314-352. [PMID: 3534538]
4. Itoh, Y. Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 7280-7290. [PMID: 9393691]
5. Stalon, V., Vander Wauven, C., Momin, P. and Legrain, C. Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria. J. Gen. Microbiol. 133 (1987) 2487-2495. [PMID: 3129535]
Accepted name: putrescine aminotransferase
Reaction: (1) putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
(2) 4-aminobutanal = 1-pyrroline (spontaneous)
For diagram click here.
Glossary: putrescine = butane-1,4-diamine
1-pyrroline = 3,4-dihydro-2H-pyrrole
Other name(s): putrescine-α-ketoglutarate transaminase; YgjG; putrescine:α-ketoglutarate aminotransferase; PAT; putrescine:2-oxoglutarate aminotransferase; putrescine transaminase
Systematic name: butane-1,4-diamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which is a substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 98982-73-1
References:
1. Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242-244. [PMID: 3510672]
2. Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107-4112. [PMID: 16023116]
3. Samsonova, N.N., Smirnov, S.V., Altman, I.B. and Ptitsyn, L.R. Molecular cloning and characterization of Escherichia coli K12 ygjG gene. BMC Microbiol. 3 (2003) 2 only. [PMID: 12617754]
Accepted name: LL-diaminopimelate aminotransferase
Reaction: LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O
For diagram click here.
Glossary: LL-diaminopimelate = LL-2,6-diaminoheptanedioate
tetrahydrodipicolinate = 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
Other name(s): LL-diaminopimelate transaminase; LL-DAP aminotransferase; LL-DAP-AT
Systematic name: LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number: 949001-34-7
References:
1. Hudson, A.O., Singh, B.K., Leustek, T. and Gilvarg, C. An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants. Plant Physiol. 140 (2006) 292-301. [PMID: 16361515]
Accepted name: arginine—pyruvate transaminase
Reaction: L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
For diagram, click here
Other name(s): arginine:pyruvate transaminase; AruH
Systematic name: L-arginine:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Yang, Z. and Lu, C.-D. Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1. J. Bacteriol. 189 (2007) 3954-3959. [PMID: 17416668]
2. Yang, Z. and Lu, C.D. Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa. J. Bacteriol. 189 (2007) 3945-3953. [PMID: 17416670]
Accepted name: aminodeoxychorismate synthase
Reaction: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
For diagram click here.
Other name(s): ADC synthase; 4-amino-4-deoxychorismate synthase; PabB; chorismate:L-glutamine amido-ligase (incorrect)
Systematic name: chorismate:L-glutamine aminotransferase
Comments: The enzyme is composed of two parts, PabA and PabB. In the absence of PabA and glutamine, PabB converts ammonia and chorismate into 4-amino-4-deoxychorismate (in the presence of Mg2+). PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. This enzyme is coupled with 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Ye, Q.Z., Liu, J. and Walsh, C.T. p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc. Natl. Acad. Sci. USA 87 (1990) 9391-9395. [PMID: 2251281]
2. Viswanathan, V.K., Green, J.M. and Nichols, B.P. Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli. J. Bacteriol. 177 (1995) 5918-5923. [PMID: 7592344]
Accepted name: 2-amino-4-deoxychorismate synthase
Reaction: (2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine
For diagram of reaction, click here
Glossary: (2S)-2-amino-4-deoxychorismate = (2S,3S)-3-(1-carboxyvinyloxy)-2,3-dihydroanthranilate
Other name(s): ADIC synthase; 2-amino-2-deoxyisochorismate synthase; SgcD
Systematic name: (2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase
Comments: Requires Mg2+. The reaction occurs in the reverse direction to that shown above. In contrast to most anthranilate-synthase I (ASI) homologues, this enzyme is not inhibited by tryptophan. In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2]. In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity [3,4].
References:
1. Van Lanen, S.G., Lin, S. and Shen, B. Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism. Proc. Natl. Acad. Sci. USA 105 (2008) 494-499. [PMID: 18182490]
2. Yu, L., Mah, S., Otani, T. and Dedon, P. The benzoxazolinate of C-1027 confers intercalative DNA binding. J. Am. Chem. Soc. 117 (1995) 8877-8878.
3. McDonald, M., Mavrodi, D.V., Thomashow, L.S. and Floss, H.G. Phenazine biosynthesis in Pseudomonas fluorescens: branchpoint from the primary shikimate biosynthetic pathway and role of phenazine-1,6-dicarboxylic acid. J. Am. Chem. Soc. 123 (2001) 9459-9460. [PMID: 11562236]
4. Laursen, J.B. and Nielsen, J. Phenazine natural products: biosynthesis, synthetic analogues, and biological activity. Chem. Rev. 104 (2004) 1663-1686. [PMID: 15008629]
Accepted name: UDP-4-amino-4-deoxy-L-arabinose aminotransferase
Reaction: UDP-4-amino-4-deoxy-β-L-arabinopyranose + 2-oxoglutarate = UDP-β-L-threo-pentapyranos-4-ulose + L-glutamate
Other name(s): UDP-(β-L-threo-pentapyranosyl-4"-ulose diphosphate) aminotransferase; UDP-4-amino-4-deoxy-L-arabinose—oxoglutarate aminotransferase; UDP-Ara4O aminotransferase; UDP-L-Ara4N transaminase
Systematic name: UDP-4-amino-4-deoxy-β-L-arabinose:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5'-phosphate enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Breazeale, S.D., Ribeiro, A.A. and Raetz, C.R. Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli. An aminotransferase (ArnB) that generates UDP-4-deoxyl-L-arabinose. J. Biol. Chem. 278 (2003) 24731-24739. [PMID: 12704196]
2. Noland, B.W., Newman, J.M., Hendle, J., Badger, J., Christopher, J.A., Tresser, J., Buchanan, M.D., Wright, T.A., Rutter, M.E., Sanderson, W.E., Muller-Dieckmann, H.J., Gajiwala, K.S. and Buchanan, S.G. Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. Structure 10 (2002) 1569-1580. [PMID: 12429098]
Accepted name: methionine transaminase
Reaction: L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + an L-amino acid
Other name(s): methionine-oxo-acid transaminase
Systematic name: L-methionine:2-oxo-acid aminotransferase
Comments: The enzyme is most active with L-methionine. It participates in the L-methionine salvage pathway from S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis. The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective [1]. The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates [3].
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Heilbronn, J., Wilson, J. and Berger, B.J. Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J. Bacteriol. 181 (1999) 1739-1747. [PMID: 10074065]
2. Dolzan, M., Johansson, K., Roig-Zamboni, V., Campanacci, V., Tegoni, M., Schneider, G. and Cambillau, C. Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. FEBS Lett. 571 (2004) 141-146. [PMID: 15280032]
3. Schuster, J., Knill, T., Reichelt, M., Gershenzon, J. and Binder, S. Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis. Plant Cell 18 (2006) 2664-2679. [PMID: 17056707]
Accepted name: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose transaminase
Reaction: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-α-D-glucopyranose + L-glutamate
Glossary: dTDP-D-mycaminose = dTDP-3-dimethylamino-3,6-dideoxy-α-D-glucopyranose
Other name(s): TylB; TDP-3-keto-6-deoxy-D-glucose 3-aminotransferase; TDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase; dTDP-3-keto-6-deoxy-D-glucose 3-aminotransferase; dTDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase
Systematic name: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The reaction occurs in the reverse direction. The enzyme is involved in biosynthesis of D-mycaminose.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Melancon, C.E., 3rd, Hong, L., White, J.A., Liu, Y.N. and Liu, H.W. Characterization of TDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from the D-mycaminose biosynthetic pathway of Streptomyces fradiae: in vitro activity and substrate specificity studies. Biochemistry 46 (2007) 577-590. [PMID: 17209568]
Accepted name: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose transaminase
Reaction: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-α-D-galactopyranose + L-glutamate
Glossary: dTDP-3-dehydro-6-deoxy-D-galactopyranose = dTDP-6-deoxy-D-xylo-hexopyranos-3-ulose
Other name(s): dTDP-6-deoxy-D-xylohex-3-uloseaminase; FdtB; TDP-3-keto-6-deoxy-D-galactose-3-aminotransferase; RavAMT; TDP-3-keto-6-deoxy-D-galactose 3-aminotransferase; TDP-3-dehydro-6-deoxy-D-galactose 3-aminotransferase
Systematic name: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-α-D-galactose. The reaction occurs in the reverse direction.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Pfoestl, A., Hofinger, A., Kosma, P. and Messner, P. Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-α-D-galactose in Aneurinibacillus thermoaerophilus L420-91T. J. Biol. Chem. 278 (2003) 26410-26417. [PMID: 12740380]
Accepted name: UDP-4-amino-4,6-dideoxy-α-D-N-acetyl-D-glucosamine transaminase
Reaction: UDP-4-amino-4,6-dideoxy-α-D-N-acetyl-D-glucosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-α-D-xylo-4-hexulose + L-glutamate
Other name(s): PglE
Systematic name: UDP-4-amino-4,6-dideoxy-α-D-N-acetyl-D-glucosamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of bacillosamine.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723-732. [PMID: 16286454]
Accepted name: UDP-4-amino-4,6-dideoxy-L-N-acetyl-β-L-altrosamine transaminase
Reaction: UDP-4-amino-4,6-dideoxy-L-N-acetyl-β-L-altrosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose + L-glutamate
Glossary: pseudaminic acid = 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid
Other name(s): PseC
Systematic name: UDP-4-amino-4,6-dideoxy-L-N-acetyl-β-L-altrosamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of pseudaminic acid.
Links to other databases: BRENDA, EXPASY, KEGG, CAS registry number:
References:
1. Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723-732. [PMID: 16286454]
2. Schoenhofen, I.C., Lunin, V.V., Julien, J.P., Li, Y., Ajamian, E., Matte, A., Cygler, M., Brisson, J.R., Aubry, A., Logan, S.M., Bhatia, S., Wakarchuk, W.W. and Young, N.M. Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori. J. Biol. Chem. 281 (2006) 8907-8916. [PMID: 16421095]