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, Metacyc, 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-phosphooxypyruvate + L-glutamate
(2) 4-phosphooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
For diagram of reaction, 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 5'-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli [3]. Pyridoxal 5'-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]. The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine [7].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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, Metacyc, 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-α-D-galactose + 2-oxoglutarate = dTDP-4-dehydro-6-deoxy-α-D-galactose + L-glutamate
For diagram of reaction click here.
Glossary: dTDP-4-dehydro-6-deoxy-α-D-galactose = dTDP-4-dehydro-6-deoxy-α-D-glucose
Other name(s): thymidine diphosphoaminodideoxygalactose aminotransferase; thymidine diphosphate 4-keto-6-deoxy-D-glucose transaminase; WecE; dTDP-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase
Systematic name: dTDP-4-amino-4,6-dideoxy-α-D-galactose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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, Metacyc, 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-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
Other name(s): 7,8-diaminonanoate transaminase; 7,8-diaminononanoate transaminase; DAPA transaminase (ambiguous); 7,8-diaminopelargonic acid aminotransferase; DAPA aminotransferase (ambiguous); 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: A pyridoxal 5′-phosphate enzyme. S-adenosylhomocysteine can also act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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: (1) L-kynurenine + glyoxylate = kynurenate + glycine + H2O (overall reaction)
(1a) L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
(1b) 4-(2-aminophenyl)-2,4-dioxobutanoate = kynurenate + H2O (spontaneous)
(2) 3-hydroxy-L-kynurenine + glyoxylate = xanthurenate + glycine + H2O (overall reaction)
(2a) 3-hydroxy-L-kynurenine + glyoxylate = 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate + glycine
(2b) 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate = xanthurenate + H2O (spontaneous)
Glossary: kynurenine = 2-amino-4-(2-aminophenyl)-4-oxobutanoic acid = 3-anthraniloylalanine
kynurenate = 4-hydroxyquinoline-2-carboxylate
xanthurenate = 4,8-dihydroxyquinoline-2-carboxylate
For diagram click here (mechanism).
Other name(s): kynurenine-glyoxylate aminotransferase
Systematic name: L-kynurenine:glyoxylate aminotransferase (cyclizing)
Comments: This enzyme, characterized from animals, belongs to a family of aminotransferases some members of which can use other amino acceptors ( cf . EC 2.6.1.7, kynurenine—oxoglutarate transaminase). The products, 4-(2-aminophenyl)-2,4-dioxobutanoate and 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate, are converted to kynurenate and xanthurenate, respectively, by spontaneous reactions.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 74506-33-5
References:
1. Harada, I., Noguchi, T. and Kido, R. Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver. Hoppe-Seylers Z. Physiol. Chem. 359 (1978) 481–488. [PMID: 25837] 2. Harada, I. [Glucagen inducible kynurenine aminotransferase.] Wakayama Igaku 31 (1980) 61–68. (in Japanese) 3. Han, Q., Fang, J. and Li, J. 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti . J. Biol. Chem. 277 (2002) 15781–15787. [PMID: 11880382] 4. Rossi, F., Lombardo, F., Paglino, A., Cassani, C., Miglio, G., Arca, B. and Rizzi, M. Identification and biochemical characterization of the Anopheles gambiae 3-hydroxykynurenine transaminase. FEBS J. 272 (2005) 5653–5662. [PMID: 16262702]
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, Metacyc, PDB, 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, Metacyc, 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, Metacyc, PDB, 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, Metacyc, 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]
[EC 2.6.1.68 Deleted entry: ornithine(lysine) transaminase. Now classified as EC 2.6.1.13, ornithine aminotransferase and EC 2.6.1.36, L-lysine 6-transaminase (EC 2.6.1.68 created 1989, deleted 2016)]
[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, Metacyc, 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, Metacyc, 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, Metacyc, PDB, 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-(methylsulfanyl)-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, Metacyc, PDB, 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, Metacyc, 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-3-[(4-bromophenyl)sulfanyl]-2-oxopropanoate + 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, Metacyc, 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 of reaction, 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, Metacyc, PDB, 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 the bacterium Bilophila wadsworthia requires pryidoxal 5'-phosphate as a cofactor and catalyses a reversible reaction that starts an anaerobic taurine degradation pathway. β-Alanine is also a significant amino group donor. The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyses to sulfite and acetaldehyde. Unlike, EC 2.6.1.55, taurine32-oxoglutarate transaminase, 2-oxoglutarate cannot serve as an acceptor for the amino group.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]
4. Felux, A.K., Denger, K., Weiss, M., Cook, A.M. and Schleheck, D. Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination followed by spontaneous desulfination to yield acetaldehyde and, finally, acetate for growth. J. Bacteriol. 195 (2013) 2921-2930. [PMID: 23603744]
Accepted name: aspartate—prephenate aminotransferase
Reaction: L-arogenate + oxaloacetate = prephenate + L-aspartate
For diagram click here, another example) (mechanism).
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, Metacyc, PDB, 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, another example) (mechanism).
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, Metacyc, PDB, 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, Metacyc, 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 of reaction, 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, Metacyc, PDB, 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—2-oxoglutarate transaminase
Reaction: putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
For diagram of reaction 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 (ambiguous); putrescine transaminase (ambiguous); putrescine aminotransferase (ambiguous); butane-1,4-diamine:2-oxoglutarate aminotransferase
Systematic name: putrescine:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5'-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual 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]. cf. EC 2.6.1.113, putrescine—pyruvate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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. [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, Metacyc, PDB, 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 of reaction click here, (another example) (mechanism).
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, Metacyc, 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 (overall reaction)
(1a) L-glutamine + H2O = L-glutamate + NH3
(1b) chorismate + NH3 = 4-amino-4-deoxychorismate + H2O
For diagram of reaction click here
Other name(s): ADC synthase; 4-amino-4-deoxychorismate synthase; PabAB; chorismate:L-glutamine amido-ligase (incorrect)
Systematic name: chorismate:L-glutamine aminotransferase
Comments: The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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]
3. Chang, Z., Sun, Y., He, J. and Vining, L.C. p-Aminobenzoic acid and chloramphenicol biosynthesis in Streptomyces venezuelae: gene sets for a key enzyme, 4-amino-4-deoxychorismate synthase. Microbiology (Reading) 147 (2001) 2113-2126. [PMID: 11495989]
4. Camara, D., Richefeu-Contesto, C., Gambonnet, B., Dumas, R. and Rebeille, F. The synthesis of pABA: Coupling between the glutamine amidotransferase and aminodeoxychorismate synthase domains of the bifunctional aminodeoxychorismate synthase from Arabidopsis thaliana. Arch. Biochem. Biophys. 505 (2011) 83-90. [PMID: 20851095]
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].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
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
For diagram of reaction click here.
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, Metacyc, PDB, 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-(methylsulfanyl)butanoate + 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, Metacyc, PDB, 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
For diagram of reaction click here.
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, Metacyc, 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-α-D-galactopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-α-D-galactopyranose + L-glutamate
For diagram of reaction click here.
Glossary: dTDP-3-dehydro-6-deoxy-α-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, Metacyc, 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]
[EC 2.6.1.91 Deleted entry: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase. Identical to EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase. (EC 2.6.1.91 created 2011, deleted 2013)]
Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine transaminase
Reaction: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose + L-glutamate
Other name(s): PseC; UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine:2-oxoglutarate aminotransferase; UDP-β-L-threo-pentapyranos-4-ulose transaminase; UDP-4-dehydro-6-deoxy-D-glucose transaminase
Systematic name: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine:2-oxoglutarate transaminase
Comments: A pyridoxal 5'-phosphate protein. The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose, UDP-β-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose. cf. EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase, which catalyses a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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]
3. Mostafavi, A.Z. and Troutman, J.M. Biosynthetic assembly of the Bacteroides fragilis capsular polysaccharide A precursor bactoprenyl diphosphate-linked acetamido-4-amino-6-deoxygalactopyranose. Biochemistry 52 (2013) 1939-1949. [PMID: 23458065]
4. Hwang, S., Li, Z., Bar-Peled, Y., Aronov, A., Ericson, J. and Bar-Peled, M. The biosynthesis of UDP-D-FucNAc-4N-(2)-oxoglutarate (UDP-Yelosamine) in Bacillus cereus ATCC 14579: Pat and Pyl, an aminotransferase and an ATP-dependent Grasp protein that ligates 2-oxoglutarate to UDP-4-amino-sugars. J. Biol. Chem 289 (2014) 35620-35632. [PMID: 25368324]
Accepted name: neamine transaminase
Reaction: neamine + 2-oxoglutarate = 6'-dehydroparomamine + L-glutamate
For diagram of reaction click here.
Other name(s): glutamate—6'-dehydroparomamine aminotransferase; btrB (gene name); neoN (gene name); kacL (gene name)
Systematic name: neamine:2-oxoglutarate aminotransferase
Comments: The reaction occurs in vivo in the opposite direction. Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin B, butirosin, neomycin and ribostamycin. Works in combination with EC 1.1.3.43, paromamine 6-oxidase, to replace the 6'-hydroxy group of paromamine with an amino group. The enzyme from the bacterium Streptomyces kanamyceticus can also catalyse EC 2.6.1.94, 2'-deamino-2'-hydroxyneamine transaminase, which leads to production of kanamycin A [3]. The enzyme from the bacterium Streptomyces fradiae can also catalyse EC 2.6.1.95, leading to production of neomycin C [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem. 8 (2007) 283-288. [PMID: 17206729]
2. Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642-651. [PMID: 21689223]
3. Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843-852. [PMID: 21983602]
Accepted name: 2'-deamino-2'-hydroxyneamine transaminase
Reaction: 2'-deamino-2'-hydroxyneamine + 2-oxoglutarate = 2'-deamino-2'-hydroxy-6'-dehydroparomamine + L-glutamate
Other name(s): kacL (gene name)
Systematic name: 2'-deamino-2'-hydroxyneamine:2-oxoglutarate aminotransferase
Comments: The reaction occurs in vivo in the opposite direction. Involved in the biosynthetic pathway of kanamycin A and kanamycin D. The enzyme, characterized from the bacterium Streptomyces kanamyceticus, can also catalyse EC 2.6.1.93, neamine transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843-852. [PMID: 21983602]
Accepted name: neomycin C transaminase
Reaction: neomycin C + 2-oxoglutarate = 6′′′-deamino-6′′′-oxoneomycin C + L-glutamate
For diagram of reaction click here.
Other name(s): neoN (gene name)
Systematic name: 2-oxoglutarate:neomycin C aminotransferase
Comments: The reaction occurs in vivo in the opposite direction. Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. Works in combination with EC 1.1.3.44, 6′′′-hydroxyneomycin C oxidase, to replace the 6′′′-hydroxy group of 6′′′-deamino-6′′′-hydroxyneomycin C with an amino group. The enzyme, characterized from the bacterium Streptomyces fradiae, can also catalyse EC 2.6.1.93, neamine transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Huang, F., Spiteller, D., Koorbanally, N.A., Li, Y., Llewellyn, N.M. and Spencer, J.B. Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin. ChemBioChem. 8 (2007) 283-288. [PMID: 17206729]
2. Clausnitzer, D., Piepersberg, W. and Wehmeier, U.F. The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin. J. Appl. Microbiol. 111 (2011) 642-651. [PMID: 21689223]
Accepted name: 4-aminobutyrate—pyruvate transaminase
Reaction: (1) 4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine
(2) 4-aminobutanoate + glyoxylate = succinate semialdehyde + glycine
Other name(s): aminobutyrate aminotransferase (ambiguous); γ-aminobutyrate aminotransaminase (ambiguous); γ-aminobutyrate transaminase (ambiguous); γ-aminobutyric acid aminotransferase (ambiguous); γ-aminobutyric acid pyruvate transaminase; γ-aminobutyric acid transaminase (ambiguous); γ-aminobutyric transaminase (ambiguous); 4-aminobutyrate aminotransferase (ambiguous); 4-aminobutyric acid aminotransferase (ambiguous); aminobutyrate transaminase (ambiguous); GABA aminotransferase (ambiguous); GABA transaminase (ambiguous); GABA transferase (ambiguous); POP2 (gene name)
Systematic name: 4-aminobutanoate:pyruvate aminotransferase
Comments: Requires pyridoxal 5'-phosphate. The enzyme is found in plants that do not have the 2-oxoglutarate dependent enzyme (cf. EC 2.6.1.19). The reaction with pyruvate is reversible while the reaction with glyoxylate only takes place in the forward direction.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Van Cauwenberghe, O.R. and Shelp, B.J. Biochemical characterization of partially purified gaba:pyruvate transaminase from Nicotiana tabacum. Phytochemistry 52 (1999) 575-581.
2. Palanivelu, R., Brass, L., Edlund, A.F. and Preuss, D. Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene that controls GABA levels. Cell 114 (2003) 47-59. [PMID: 12859897]
3. Clark, S.M., Di Leo, R., Dhanoa, P.K., Van Cauwenberghe, O.R., Mullen, R.T. and Shelp, B.J. Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis γ-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate. J. Exp. Bot. 60 (2009) 1743-1757. [PMID: 19264755]
4. Clark, S.M., Di Leo, R., Van Cauwenberghe, O.R., Mullen, R.T. and Shelp, B.J. Subcellular localization and expression of multiple tomato γ-aminobutyrate transaminases that utilize both pyruvate and glyoxylate. J. Exp. Bot. 60 (2009) 3255-3267. [PMID: 19470656]
Accepted name: archaeosine synthase
Reaction: L-glutamine + 7-cyano-7-carbaguanine15 in tRNA + H2O = L-glutamate + archaeine15 in tRNA
Glossary: 7-cyano-7-carbaguanine = preQ0 = 7-cyano-7-deazaguanine
archaeine = 7-deaza-7-carbamidoylguanine = base G*
archaeosine = G* = 7-amidino-7-deazaguanosine
Other name(s): ArcS; TgtA2; MJ1022 (gene name); glutamine:preQ0-tRNA amidinotransferase (incorrect)
Systematic name: L-glutamine:7-cyano-7-carbaguanine aminotransferase
Comments: In Euryarchaeota the reaction is catalysed by ArcS [1,2]. In Crenarchaeota, which do not have an ArcS homologue, the reaction is catalysed either by a homologue of EC 6.3.4.20, 7-cyano-7-deazaguanine synthase that includes a glutaminase domain (cf. EC 3.5.1.2), or by a homologue of EC 1.7.1.13, preQ1 synthase [2]. The enzyme from the Euryarchaeon Methanocaldococcus jannaschii can also use arginine and ammonium as amino donors.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Phillips, G., Chikwana, V.M., Maxwell, A., El-Yacoubi, B., Swairjo, M.A., Iwata-Reuyl, D. and de Crecy-Lagard, V. Discovery and characterization of an amidinotransferase involved in the modification of archaeal tRNA. J. Biol. Chem. 285 (2010) 12706-12713. [PMID: 20129918]
2. Phillips, G., Swairjo, M.A., Gaston, K.W., Bailly, M., Limbach, P.A., Iwata-Reuyl, D. and de Crecy-Lagard, V. Diversity of archaeosine synthesis in crenarchaeota. ACS Chem. Biol. 7 (2012) 300-305. [PMID: 22032275]
Accepted name: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
Reaction: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate + 2-oxoglutarate = UDP-2-acetamido-2-deoxy-D-ribo-hex-3-uluronate + L-glutamate
For diagram of reaction, click here
Other name(s): WbpE; WlbC
Systematic name: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5'-phosphate protein. This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the previous enzyme in the pathway, EC 1.1.1.335 (UDP-N-acetyl-2-amino-2-deoxyglucuronate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854-11862. [PMID: 19282284]
2. Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446-5455. [PMID: 19348502]
3. Larkin, A., Olivier, N.B. and Imperiali, B. Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly. Biochemistry 49 (2010) 7227-7237. [PMID: 20604544]
Accepted name: L-tryptophan—pyruvate aminotransferase
Reaction: L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine
For diagram of reaction click here, another example) (mechanism).
Other name(s): TAA1 (gene name); vt2 (gene name)
Systematic name: L-tryptophan:pyruvate aminotransferase
Comments: This plant enzyme, along with EC 1.14.13.168, indole-3-pyruvate monooxygenase, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tao, Y., Ferrer, J.L., Ljung, K., Pojer, F., Hong, F., Long, J.A., Li, L., Moreno, J.E., Bowman, M.E., Ivans, L.J., Cheng, Y., Lim, J., Zhao, Y., Ballare, C.L., Sandberg, G., Noel, J.P. and Chory, J. Rapid synthesis of auxin via a new tryptophan-dependent pathway is required for shade avoidance in plants. Cell 133 (2008) 164-176. [PMID: 18394996]
2. Mashiguchi, K., Tanaka, K., Sakai, T., Sugawara, S., Kawaide, H., Natsume, M., Hanada, A., Yaeno, T., Shirasu, K., Yao, H., McSteen, P., Zhao, Y., Hayashi, K., Kamiya, Y. and Kasahara, H. The main auxin biosynthesis pathway in Arabidopsis. Proc. Natl. Acad. Sci. USA 108 (2011) 18512-18517. [PMID: 22025724]
3. Phillips, K.A., Skirpan, A.L., Liu, X., Christensen, A., Slewinski, T.L., Hudson, C., Barazesh, S., Cohen, J.D., Malcomber, S. and McSteen, P. vanishing tassel2 encodes a grass-specific tryptophan aminotransferase required for vegetative and reproductive development in maize. Plant Cell 23 (2011) 550-566. [PMID: 21335375]
4. Zhao, Y. Auxin biosynthesis: a simple two-step pathway converts tryptophan to indole-3-acetic acid in plants. Mol. Plant 5 (2012) 334-338. [PMID: 22155950]
Accepted name: L-glutamine:2-deoxy-scyllo-inosose aminotransferase
Reaction: L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo-inosamine
For diagram of reaction click here.
Glossary: 2-deoxy-scyllo-inosose = (2S,3R,4S,5R)-2,3,4,5-tetrahydroxycyclohexan-1-one
Other name(s): btrR (gene name); neoB (gene name); kanB (gene name)
Systematic name: L-glutamine:2-deoxy-scyllo-inosose aminotransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.101, L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tamegai, H., Eguchi, T. and Kakinuma, K. First identification of Streptomyces genes involved in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics--genetic and evolutionary analysis of L-glutamine:2-deoxy-scyllo-inosose aminotransferase genes. J. Antibiot. (Tokyo) 55 (2002) 1016-1018. [PMID: 12546424]
2. Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410-1418. [PMID: 15827636]
3. Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766-774. [PMID: 16506694]
4. Jnawali, H.N., Subba, B., Liou, K. and Sohng, J.K. Functional characterization of kanB by complementing in engineered Streptomyces fradiae Δneo6::tsr. Biotechnol. Lett. 31 (2009) 869-875. [PMID: 19219581]
Accepted name: L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
Reaction: L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine
For diagram of reaction click here.
Glossary: 3-amino-2,3-dideoxy-scyllo-inosose = (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexan-1-one
Systematic name: L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.100, L-glutamine:2-deoxy-scyllo-inosose aminotransferase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410-1418. [PMID: 15827636]
2. Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766-774. [PMID: 16506694]
Accepted name: GDP-perosamine synthase
Reaction: GDP-α-D-perosamine + 2-oxoglutarate = GDP-4-dehydro-α-D-rhamnose + L-glutamate
Glossary: GDP-α-D-perosamine = GDP-4-amino-4,6-dideoxy-α-D-mannose
GDP-4-dehydro-α-D-rhamnose = GDP-4-dehydro-6-deoxy-α-D-mannose
Other name(s): RfbE; GDP-4-keto-6-deoxy-D-mannose-4-aminotransferase; GDP-perosamine synthetase; PerA; GDP-4-amino-4,6-dideoxy-α-D-mannose:2-oxoglutarate aminotransferase
Systematic name: GDP-α-D-perosamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5′-phosphate enzyme. D-Perosamine is one of several dideoxy sugars found in the O-specific polysaccharide of the lipopolysaccharide component of the outer membrane of Gram-negative bacteria. The enzyme catalyses the final step in GDP-α-D-perosamine synthesis.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Albermann, C. and Piepersberg, W. Expression and identification of the RfbE protein from Vibrio cholerae O1 and its use for the enzymatic synthesis of GDP-D-perosamine. Glycobiology 11 (2001) 655-661. [PMID: 11479276]
2. Zhao, G., Liu, J., Liu, X., Chen, M., Zhang, H. and Wang, P.G. Cloning and characterization of GDP-perosamine synthetase (Per) from Escherichia coli O157:H7 and synthesis of GDP-perosamine in vitro. Biochem. Biophys. Res. Commun. 363 (2007) 525-530. [PMID: 17888872]
3. Albermann, C. and Beuttler, H. Identification of the GDP-N-acetyl-d-perosamine producing enzymes from Escherichia coli O157:H7. FEBS Lett 582 (2008) 479-484. [PMID: 18201574]
4. Cook, P.D., Carney, A.E. and Holden, H.M. Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase. Biochemistry 47 (2008) 10685-10693. [PMID: 18795799]
Accepted name: (S)-3,5-dihydroxyphenylglycine transaminase
Reaction: (S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + L-glutamate
Glossary: (S)-3,5-dihydroxyphenylglycine = (2S)-2-amino-2-(3,5-dihydroxyphenyl)acetic acid
Other name(s): HpgT
Systematic name: (S)-3,5-dihydroxyphenylglycine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-5′-phosphate protein. The enzyme from the bacterium Amycolatopsis orientalis catalyses the reaction in the reverse direction as part of the biosynthesis of the (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Sandercock, A.M., Charles, E.H., Scaife, W., Kirkpatrick, P.N., O'Brien, S.W., Papageorgiou, E.A., Spencer, J.B. and Williams, D.H. Biosynthesis of the di-meta-hydroxyphenylglycine constituent of the vancomycin-group antibiotic chloroeremomycin. Chem. Comm. (2001) 1252-1253.
Accepted name: 3-dehydro-glucose-6-phosphate—glutamate transaminase
Reaction: kanosamine 6-phosphate + 2-oxoglutarate = 3-dehydro-D-glucose 6-phosphate + L-glutamate
For diagram of reaction click here.
Glossary: kanosamine = 3-amino-3-deoxy-D-glucose
Other name(s): 3-oxo-glucose-6-phosphate:glutamate aminotransferase; ntdA (gene name)
Systematic name: kanosamine 6-phosphate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme, found in the bacterium Bacillus subtilis, is involved in a kanosamine biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. van Straaten, K.E., Langill, D.M., Palmer, D.R. and Sanders, D.A. Purification, crystallization and preliminary X-ray analysis of NtdA, a putative pyridoxal phosphate-dependent aminotransferase from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 426-429. [PMID: 19342798]
2. Vetter, N.D., Langill, D.M., Anjum, S., Boisvert-Martel, J., Jagdhane, R.C., Omene, E., Zheng, H., van Straaten, K.E., Asiamah, I., Krol, E.S., Sanders, D.A. and Palmer, D.R. A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. J. Am. Chem. Soc. 135 (2013) 5970-5973. [PMID: 23586652]
Accepted name: lysine—8-amino-7-oxononanoate transaminase
Reaction: L-lysine + 8-amino-7-oxononanoate = (S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): DAPA aminotransferase (ambiguous); bioA (gene name) (ambiguous); bioK (gene name)
Systematic name: L-lysine:8-amino-7-oxononanoate aminotransferase
Comments: A pyridoxal 5'-phosphate enzyme [2]. Participates in the pathway for biotin biosynthesis. The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyses an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62, adenosylmethionine—8-amino-7-oxononanoate transaminase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Van Arsdell, S.W., Perkins, J.B., Yocum, R.R., Luan, L., Howitt, C.L., Chatterjee, N.P. and Pero, J.G. Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction. Biotechnol. Bioeng. 91 (2005) 75-83. [PMID: 15880481]
2. Dey, S., Lane, J.M., Lee, R.E., Rubin, E.J. and Sacchettini, J.C. Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase. Biochemistry 49 (2010) 6746-6760. [PMID: 20565114]
Accepted name: dTDP-3-amino-3,4,6-trideoxy-α-D-glucose transaminase
Reaction: dTDP-3-amino-3,4,6-trideoxy-α-D-glucose + 2-oxoglutarate = dTDP-3-dehydro-4,6-deoxy-α-D-glucose + L-glutamate
For diagram of reaction click here.
Glossary: dTDP-α-D-desosamine = dTDP-3-(dimethylamino)-3,4,6-trideoxy-α-D-glucose
Other name(s): desV (gene name); megDII (gene name); eryCI (gene name)
Systematic name: dTDP-3-amino-3,4,6-trideoxy-α-D-glucose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in the biosynthesis of dTDP-α-D-desosamine, a sugar found in several bacterial macrolide antibiotics including erythromycin, megalomicin A, mycinamicin II, and oleandomycin. The reaction occurs in the reverse direction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Burgie, E.S., Thoden, J.B. and Holden, H.M. Molecular architecture of DesV from Streptomyces venezuelae: a PLP-dependent transaminase involved in the biosynthesis of the unusual sugar desosamine. Protein Sci. 16 (2007) 887-896. [PMID: 17456741]
Accepted name: β-methylphenylalanine transaminase
Reaction: (2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-phenylbutanoate + L-glutamate
Glossary: (3S)-2-oxo-3-phenylbutanoate = (3S)-β-methyl-phenylpyruvate
Other name(s): TyrB
Systematic name: (2S,3S)-3-methylphenylalanine:2-oxoglutarate aminotransferase
Comments: Requires pyridoxal phosphate. Isolated from the bacterium Streptomyces hygroscopicus NRRL3085. It is involved in the biosynthesis of the glycopeptide antibiotic mannopeptimycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Huang, Y.T., Lyu, S.Y., Chuang, P.H., Hsu, N.S., Li, Y.S., Chan, H.C., Huang, C.J., Liu, Y.C., Wu, C.J., Yang, W.B. and Li, T.L. In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-β-methylphenylalanine in glycopeptide antibiotic mannopeptimycin. Chembiochem 10 (2009) 2480-2487. [PMID: 19731276]
Accepted name: (5-formylfuran-3-yl)methyl phosphate transaminase
Reaction: L-alanine + (5-formylfuran-3-yl)methyl phosphate = pyruvate + [5-(aminomethyl)furan-3-yl]methyl phosphate
For diagram of reaction click here.
Other name(s): mfnC (gene name); [5-(hydroxymethyl)furan-3-yl]methyl phosphate transaminase
Systematic name: L-alanine:(5-formylfuran-3-yl)methyl phosphate aminotransferase
Comments: A pyridoxal 5'-phosphate protein. The enzyme, characterized from the archaebacterium Methanocaldococcus jannaschii, participates in the biosynthesis of the cofactor methanofuran. Requires pyridoxal 5'-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Miller, D., Wang, Y., Xu, H., Harich, K. and White, R.H. Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of methanofuran. Biochemistry 53 (2014) 4635-4647. [PMID: 24977328]
Accepted name: 8-amino-3,8-dideoxy-α-D-manno-octulosonate transaminase
Reaction: 8-amino-3,8-dideoxy-α-D-manno-octulosonate + 2-oxoglutarate = 8-dehydro-3-deoxy-α-D-manno-octulosonate + L-glutamate
Glossary: 3-deoxy-α-D-manno-octulosonate = Kdo
8-dehydro-3-deoxy-α-D-manno-octulosonate = (2R,4R,5R,6S)-2,4,5-trihydroxy-6-[(1S)-1-hydroxy-2-oxoethyl]oxane-2-carboxylate
Other name(s): kdnA (gene name)
Systematic name: 8-amino-3,8-dideoxy-α-D-manno-octulosonate:2-oxoglutarate aminotransferase
Comments: The enzyme, characterized from the bacterium Shewanella oneidensis, forms 8-amino-3,8-dideoxy-α-D-manno-octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus. cf. EC 1.1.3.48, 3-deoxy-α-D-manno-octulosonate 8-oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Gattis, S.G., Chung, H.S., Trent, M.S. and Raetz, C.R. The origin of 8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) in the lipopolysaccharide of Shewanella oneidensis. J. Biol. Chem. 288 (2013) 9216-9225. [PMID: 23413030]
Accepted name: dTDP-4-dehydro-2,3,6-trideoxy-D-glucose 4-aminotransferase
Reaction: dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose + 2-oxoglutarate = dTDP-4-dehydro-2,3,6-trideoxy-α-D-hexopyranose + L-glutamate
For diagram of reaction click here.
Other name(s): SpnR; TDP-4-keto-2,3,6-trideoxy-D-glucose 4-aminotransferase
Systematic name: dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme, isolated from the bacterium Saccharopolyspora spinosa, participates in the biosynthesis of forosamine.
References:
1. Hong, L., Zhao, Z., Melancon, C.E., 3rd, Zhang, H. and Liu, H.W. In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa, J. Am. Chem. Soc. 130 (2008) 4954-4967. [PMID: 18345667]
Accepted name: 3-aminobutanoyl-CoA transaminase
Reaction: 3-aminobutanoyl-CoA + 2-oxoglutarate = acetoacetyl-CoA + L-glutamate
Other name(s): kat (gene name); acyl-CoA β-transaminase
Systematic name: 3-aminobutanoyl-CoA:2-oxoglutarate aminotransferase
Comments: The enzyme, found in bacteria, is part of a L-lysine degradation pathway. The enzyme is also active with other β-amino compounds such as 3-amino-5-methylhexanoyl-CoA and 3-amino-3-phenylpropanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Perret, A., Lechaplais, C., Tricot, S., Perchat, N., Vergne, C., Pelle, C., Bastard, K., Kreimeyer, A., Vallenet, D., Zaparucha, A., Weissenbach, J. and Salanoubat, M. A novel acyl-CoA β-transaminase characterized from a metagenome. PLoS One 6 (2011) e22918. [PMID: 21826218]
Accepted name: (S)-ureidoglycine—glyoxylate transaminase
Reaction: (S)-ureidoglycine + glyoxylate = N-carbamoyl-2-oxoglycine + glycine
Glossary: (S)-ureidoglycine = (2S)-(carbamoylamino)glycine
Other name(s): (S)-ureidoglycine—glyoxylate aminotransferase; UGXT; PucG
Systematic name: (S)-ureidoglycine:glyoxylate aminotransferase
Comments: A pyridoxal 5'-phosphate protein. The protein, found in bacteria, can use other amino-group acceptors, but is specific for (S)-ureidoglycine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Ramazzina, I., Costa, R., Cendron, L., Berni, R., Peracchi, A., Zanotti, G. and Percudani, R. An aminotransferase branch point connects purine catabolism to amino acid recycling. Nat. Chem. Biol. 6 (2010) 801-806. [PMID: 20852637]
Accepted name: putrescine—pyruvate transaminase
Reaction: putrescine + pyruvate = 4-aminobutanal + alanine
Other name(s): spuC (gene name)
Systematic name: putrescine:pyruvate aminotransferase
Comments: A pyridoxal 5'-phosphate protein. The enzyme, studied in the bacterium Pseudomonas aeruginosa, participates in a putrescine degradation pathway. cf. EC 2.6.1.82, putrescine—2-oxoglutarate aminotransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lu, C.D., Itoh, Y., Nakada, Y. and Jiang, Y. Functional analysis and regulation of the divergent spuABCDEFGH-spuI operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAO1. J. Bacteriol. 184 (2002) 3765-3773. [PMID: 12081945]
Accepted name: 8-demethyl-8-aminoriboflavin-5′-phosphate synthase
Reaction: L-glutamate + FMN + O2 + H2O + 3 acceptor = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5′-phosphate + CO2 + 3 reduced acceptor (overall reaction)
(1a) FMN + O2 = 8-demethyl-8-formylriboflavin 5′-phosphate + H2O
(1b) 8-demethyl-8-formylriboflavin 5′-phosphate + H2O + acceptor = 8-carboxy-8-demethylriboflavin 5′-phosphate + reduced acceptor
(1c) L-glutamate + 8-carboxy-8-demethylriboflavin 5′-phosphate + H2O + 2 acceptor = 2-oxoglutarate + 8-amino-8-demethylriboflavin 5′-phosphate + CO2 + 2 reduced acceptor
For diagram of reaction click here.
Glossary: roseoflavin = 8-demethyl-8-(dimethylamino)riboflavin
Other name(s): rosB (gene name)
Systematic name: L-glutamate:FMN aminotransferase (oxidizing, decarboxylating)
Comments: The enzyme, characterized from the bacterium Streptomyces davawensis, has the activities of an oxidoreductase, a decarboxylase, and an aminotransferase. Its combined actions result in the replacement of a methyl substituent of one of the aromatic rings of FMN by an amino group, a step in the biosynthetic pathway of roseoflavin. The reaction requires thiamine for completion.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Schwarz, J., Konjik, V., Jankowitsch, F., Sandhoff, R. and Mack, M. Identification of the key enzyme of roseoflavin biosynthesis. Angew Chem Int Ed Engl 55 (2016) 6103-6106. [PMID: 27062037]
2. Jhulki, I., Chanani, P.K., Abdelwahed, S.H. and Begley, T.P. A remarkable oxidative cascade that replaces the riboflavin C8 methyl with an amino group during roseoflavin biosynthesis. J. Am. Chem. Soc. 138 (2016) 8324-8327. [PMID: 27331868]
3. Konjik, V., Brunle, S., Demmer, U., Vanselow, A., Sandhoff, R., Ermler, U. and Mack, M. The crystal structure of RosB: insights into the reaction mechanism of the first member of a family of flavodoxin-like enzymes. Angew Chem Int Ed Engl 56 (2017) 1146-1151. [PMID: 27981706]
Accepted name: 5-hydroxydodecatetraenal 1-aminotransferase
Reaction: (2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol + pyruvate = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + L-alanine
For diagram of reaction click here.
Glossary: coelimycin P1 = N-[(3R)-8-[(2E)-but-2-enoyl]-2-oxo-6-[(2E)-1,2,5,6-tetrahydropyridin-2-ylidene]-2,3,4,6-tetrahydro-1,5-oxathiocin-3-yl]acetamide
Other name(s): cpkG (gene name)
Systematic name: (2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol:pyruvate aminotransferase
Comments: The enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), participates in the biosynthesis of coelimycin P1, where it catalyses the amination of (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal. L-glutamate can also serve as the amino group donor with lower efficiency.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, CAS registry number:
References:
1. Pawlik, K., Kotowska, M., Chater, K.F., Kuczek, K. and Takano, E. A cryptic type I polyketide synthase (cpk) gene cluster in Streptomyces coelicolor A3(2). Arch. Microbiol. 187 (2007) 87-99. [PMID: 17009021]
2. Awodi, U.R., Ronan, J.L., Masschelein, J., Santos, E.LC. and Challis, G.L. Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis. Chem. Sci. 8 (2017) 411-415. [PMID: 28451186]
Accepted name: 6-aminohexanoate aminotransferase
Reaction: 6-aminohexanoate + 2-oxoglutarate = 6-oxohexanoate + L-glutamate
Other name(s): nylD (gene name)
Systematic name: 6-aminohexanoate:2-oxogutarate aminotransferase
Comments: The enzyme, characterized from the bacterium Arthrobacter sp. KI72, participates in the degradation of nylon-6. Glyoxylate can serve as an alternative amino group acceptor with similar efficiency.
References:
1. Takehara, I., Fujii, T., Tanimoto, Y., Kato, D.I., Takeo, M. and Negoro, S. Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate. Appl. Microbiol. Biotechnol. 102 (2018) 801-814. [PMID: 29188330]
Accepted name: L-glutamine—4-(methylsulfanyl)-2-oxobutanoate aminotransferase
Reaction: L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate = 2-oxoglutaramate + L-methionine
Other name(s): mtnE (gene name); Solyc11g013170.1 (locus name)
Systematic name: L-glutamine:4-(methylsulfanyl)-2-oxobutanoate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme, found in both prokaryotes and eukaryotes, catalyses the last reaction in a methionine salvage pathway. In mammals this activity is catalysed by the multifunctional glutamine transaminase K (cf. EC 2.6.1.64, glutamine–phenylpyruvate transaminase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Berger, B.J., English, S., Chan, G. and Knodel, M.H. Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J. Bacteriol. 185 (2003) 2418-2431. [PMID: 12670965]
2. Ellens, K.W., Richardson, L.G., Frelin, O., Collins, J., Ribeiro, C.L., Hsieh, Y.F., Mullen, R.T. and Hanson, A.D. Evidence that glutamine transaminase and ω-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants. Phytochemistry 113 (2015) 160-169. [PMID: 24837359]
Accepted name: [amino group carrier protein]-γ-(L-lysyl)-L-glutamate aminotransferase
Reaction: an [amino group carrier protein]-C-terminal-γ-(L-lysyl)-L-glutamate + 2-oxoglutarate = an [amino group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
Other name(s): lysJ (gene name)
Systematic name: 2-oxoglutarate:[amino group carrier protein]-C-terminal-γ-(L-lysyl)-L-glutamate aminotransferase
Comments: The enzyme participates in an L-lysine biosynthesis pathway in certain species of archaea and bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Miyazaki, J., Kobashi, N., Nishiyama, M. and Yamane, H. Functional and evolutionary relationship between arginine biosynthesis and prokaryotic lysine biosynthesis through α-aminoadipate. J. Bacteriol. 183 (2001) 5067-5073. [PMID: 11489859]
2. Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673-679. [PMID: 19620981]
Accepted name: vanillin aminotransferase
Reaction: L-alanine + vanillin = pyruvate + vanillylamine
Other name(s): VAMT (gene name)
Systematic name: L-alanine:vanillin aminotransferase
Comments: The enzyme participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum sp. In vivo it has only been assayed in the reverse direction, where the preferred amino group acceptors were found to be pyruvate and oxaloacetate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Curry, J., Aluru, M., Mendoza, M., Nevarez, J., Melendrez, M. and O'Connell, M.A. Transcripts for possible capsaicinoid biosynthetic genes are differentially accumulated in pungent and non-pungent Capsicum spp. Plant Sci. 148 (1999) 47-57.
2. del Rosario Abraham-Juarez, M., del Carmen Rocha-Granados, M., Lopez, M.G., Rivera-Bustamante, R.F. and Ochoa-Alejo, N. Virus-induced silencing of Comt, pAmt and Kas genes results in a reduction of capsaicinoid accumulation in chili pepper fruits. Planta 227 (2008) 681-695. [PMID: 17999078]
3. Lang, Y., Kisaka, H., Sugiyama, R., Nomura, K., Morita, A., Watanabe, T., Tanaka, Y., Yazawa, S. and Miwa, T. Functional loss of pAMT results in biosynthesis of capsinoids, capsaicinoid analogs, in Capsicum annuum cv. CH-19 Sweet. Plant J. 59 (2009) 953-961. [PMID: 19473323]
4. Gururaj, H.B., Padma, M.N., Giridhar, P. and Ravishankar, G.A. Functional validation of Capsicum frutescens aminotransferase gene involved in vanillylamine biosynthesis using Agrobacterium mediated genetic transformation studies in Nicotiana tabacum and Capsicum frutescens calli cultures. Plant Sci. 195 (2012) 96-105. [PMID: 22921003]
5. Weber, N., Ismail, A., Gorwa-Grauslund, M. and Carlquist, M. Biocatalytic potential of vanillin aminotransferase from Capsicum chinense. BMC Biotechnol 14 (2014) 25. [PMID: 24712445]
Accepted name: β-alanine—2-oxoglutarate transaminase
Reaction: β-alanine + 2-oxoglutarate = 3-oxopropanoate + L-glutamate
For diagram of reaction, click here
Other name(s): pydD (gene name); β-alanine aminotransferase
Systematic name: β-alanine:2-oxoglutarate aminotransferase
Comments: The enzyme, found in many Gram-positive bacteria, participates in the reductive degradation of pyrimidines. In eukaryotes this activity is catalysed by EC 2.6.1.19, 4-aminobutyrate—2-oxoglutarate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Fujimoto, S., Mizutani, N., Mizota, C. and Tamaki, N. The level of β-alanine aminotransferase activity in regenerating and differentiating rat liver. Biochim. Biophys. Acta 882 (1986) 106-112. [PMID: 3085724]
2. Yin, J., Wei, Y., Liu, D., Hu, Y., Lu, Q., Ang, E.L., Zhao, H. and Zhang, Y. An extended bacterial reductive pyrimidine degradation pathway that enables nitrogen release from β-alanine. J. Biol. Chem. 294 (2019) 15662-15671. [PMID: 31455636]
Accepted name: 8-amino-7-oxononanoate carboxylating dehydrogenase
Reaction: (8S)-8-amino-7-oxononanoate + [protein]-L-lysine + CO2 = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate (overall reaction)
(1a) (8S)-8-amino-7-oxononanoate + [protein]-L-lysine + NAD(P)H = [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + H2O + NAD(P)+
(1b) [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + CO2 + H2O + NAD(P)+ + H+ = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate + NAD(P)H + H+
Other name(s): bioU (gene name)
Systematic name: (8S)-8-amino-7-oxononanoate:[protein]-L-lysine aminotransferase (N-carboxylating)
Comments: The enzyme, which participates in biotin biosynthesis, is found in haloarchaea and some cyanobacteria. It forms a conjugant between (7R,8S)-8-amino-7-oxononanoate and an internal lysine residue and catalyses multiple reactions, including a reduction, a carboxylation of the ε-amino group of the lysine residue, and an oxidative cleavage of the conjugate to release (7R,8S)-8-amino-7-(carboxyamino)nonanoate. During this process the lysine residue serves as an amino donor and is converted to (S)-2-amino-6-oxohexanoate, resulting in inactivation of the enzyme following a single turnover. cf. EC 2.6.1.105, lysine—8-amino-7-oxononanoate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sakaki, K., Ohishi, K., Shimizu, T., Kobayashi, I., Mori, N., Matsuda, K., Tomita, T., Watanabe, H., Tanaka, K., Kuzuyama, T. and Nishiyama, M. A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria. Nat. Chem. Biol. 16 (2020) 415-422. [PMID: 32042199]
Accepted name: UDP-N-acetyl-3-dehydro-α-D-glucosamine 3-aminotranferase
Reaction: UDP-3-acetamido-2-amino-2,3-dideoxy-α-D-glucopyranose + 2-oxoglutarate = UDP-N-acetyl-3-dehydro-α-D-glucosamine + L-glutamate
Other name(s): gnnB (gene name)
Systematic name: UDP-3-acetamido-2-amino-2,3-dideoxy-α-D-glucopyranose:2-oxoglutarate aminotransferase
Comments: This bacterial enzyme participates, together with EC 1.1.1.374, UDP-N-acetylglucosamine 3-dehydrogenase, in the synthesis of 2,3-diamino-2,3-dideoxy-D-glucopyranose, a component of lipid A in some species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sweet, C.R., Ribeiro, A.A. and Raetz, C.R. Oxidation and transamination of the 3"-position of UDP-N-acetylglucosamine by enzymes from Acidithiobacillus ferrooxidans. Role in the formation of lipid a molecules with four amide-linked acyl chains. J. Biol. Chem. 279 (2004) 25400-25410. [PMID: 15044494]
Accepted name: 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming)
Reaction: chorismate + 2 L-glutamine + H2O = 4-amino-4-deoxychorismate + 2 L-glutamate + NH3 (overall reaction)
(1a) 2 L-glutamine + 2 H2O = 2 L-glutamate + 2 NH3
(1b) chorismate + NH3 = (2S)-2-amino-4-deoxychorismate + H2O
(1c) (2S)-2-amino-4-deoxychorismate + NH3 = 4-amino-4-deoxychorismate + NH3
Other name(s): ADCS (ambiguous); ADC synthase (ambiguous)
Systematic name: chorismate:L-glutamine aminotransferase (2-amino-4-deoxychorismate-forming)
Comments: The enzyme, characterized from the bacterium Bacillus subtilis, is a heterodimer. The PabA component is a glutamine amidotransferase that hydrolyses glutamine to glutamate, forming ammonia, which is channeled to the PabB active site. PabB catalyses the formation of 4-amino-4-deoxychorismate from chorismate in two steps, via the intermediate 2-amino-4-deoxychorismate. cf. EC 2.6.1.85, aminodeoxychorismate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Schadt, H.S., Schadt, S., Oldach, F. and Sussmuth, R.D. 2-Amino-2-deoxyisochorismate is a key intermediate in Bacillus subtilis p-aminobenzoic acid biosynthesis. J. Am. Chem. Soc. 131 (2009) 3481-3483. [PMID: 19275258]
2. Bera, A.K., Atanasova, V., Dhanda, A., Ladner, J.E. and Parsons, J.F. Structure of aminodeoxychorismate synthase from Stenotrophomonas maltophilia, Biochemistry 51 (2012) 10208-10217. [PMID: 23230967]
Accepted name: [amino-group carrier protein]-γ-(L-ornithyl)-L-glutamate aminotransferase
Reaction: an [amino-group carrier protein]-C-terminal-[γ-(L-ornithyl)-L-glutamate] + 2-oxoglutarate = an [amino-group carrier protein]-C-terminal-[γ-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate] + L-glutamate
Other name(s): lysJ (gene name)
Systematic name: 2-oxoglutarate:[amino-group carrier protein]-C-terminal-[γ-(L-ornithyl)-L-glutamate] aminotransferase
Comments: The enzyme participates in an L-arginine biosynthetic pathway that operates in certain species of archaea. In some cases the enzyme also catalyses the activity of EC 2.6.1.118, [amino-group carrier protein]-γ-(L-lysyl)-L-glutamate aminotransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630-21643. [PMID: 27566549]
Accepted name: L-arginine:2-oxoglutarate transaminase
Reaction: L-arginine + 2-oxoglutarate = 5-guanidino-2-oxopentanoate + L-glutamate
Other name(s): argM (gene name); arginine-α-ketoglutarate transaminase
Systematic name: L-arginine:2-oxoglutarate aminotransferase
Comments: Requires pyridoxal 5'-phosphate. The enzyme, characterized from several bacterial species, is known to participate in L-arginine degradation and in the biosynthesis of the rare amino acid (3R)-3-methyl-L-arginine. The enzyme from Streptomyces arginensis also catalyses the activity of EC 2.6.1.126, L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Tachiki, T., Kohno, H., Sugiyama, K., Matsubara, T. and Tochikura, T. Purification, properties and formation of arginine-α-ketoglutarate transaminase in Arthrobacter simplex. Biochim. Biophys Acta 615 (1980) 79-84. [PMID: 7426667]
2. Feng, J., Wu, J., Gao, J., Xia, Z., Deng, Z. and He, X. Biosynthesis of the β-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941. Appl. Environ. Microbiol. 80 (2014) 5021-5027. [PMID: 24907335]
Accepted name: L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase
Reaction: L-aspartate + (3R)-5-guanidino-3-methyl-2-oxopentanoate = oxaloacetate + (3R)-3-methyl-L-arginine
Other name(s): argM (gene name); mrsB (gene name)
Systematic name: L-aspartate:5-guanidino-3-methyl-2-oxopentanoate aminotransferase
Comments: Requires pyridoxal 5'-phosphate. The enzyme, characterized from several bacterial species, participates in the biosynthesis of the rare amino acid (3R)-3-methyl-L-arginine. The enzyme from Streptomyces arginensis also catalyses the activity of EC 2.6.1.125, L-arginine:2-oxoglutarate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Braun, S.D., Hofmann, J., Wensing, A., Ullrich, M.S., Weingart, H., Völksch, B. and Spiteller, D. Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93. Appl. Environ. Microbiol. 76 (2010) 2500-2508. [PMID: 20190091]
2. Feng, J., Wu, J., Gao, J., Xia, Z., Deng, Z. and He, X. Biosynthesis of the β-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941. Appl. Environ. Microbiol. 80 (2014) 5021-5027. [PMID: 24907335]