Enzyme Nomenclature

EC 2.6.1 Transaminase (Continued)

Continued from EC 2.6.1.1 to EC 2.6.1.50

Contents

EC 2.6.1.51 serine—pyruvate transaminase
EC 2.6.1.52 phosphoserine transaminase
EC 2.6.1.53 now EC 1.4.1.13
EC 2.6.1.54 pyridoxamine-phosphate transaminase
EC 2.6.1.55 taurine transaminase
EC 2.6.1.56 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase
EC 2.6.1.57 aromatic-amino-acid transaminase
EC 2.6.1.58 phenylalanine(histidine) transaminase
EC 2.6.1.59 dTDP-4-amino-4,6-dideoxygalactose transaminase
EC 2.6.1.60 aromatic-amino-acid—glyoxylate transaminase
EC 2.6.1.61 identical to EC 2.6.1.40
EC 2.6.1.62 adenosylmethionine—8-amino-7-oxononanoate transaminase
EC 2.6.1.63 kynurenine—glyoxylate transaminase
EC 2.6.1.64 glutamine—phenylpyruvate transaminase
EC 2.6.1.65 N6-acetyl-β-lysine transaminase
EC 2.6.1.66 valine—pyruvate transaminase
EC 2.6.1.67 2-aminohexanoate transaminase
EC 2.6.1.68 deleted, covered by EC 2.6.1.13 and EC 2.6.1.36
EC 2.6.1.69 now EC 2.6.1.11
EC 2.6.1.70 aspartate—phenylpyruvate transaminase
EC 2.6.1.71 lysine—pyruvate 6-transaminase
EC 2.6.1.72 D-4-hydroxyphenylglycine transaminase
EC 2.6.1.73 methionine—glyoxylate transaminase
EC 2.6.1.74 cephalosporin-C transaminase
EC 2.6.1.75 cysteine-conjugate transaminase
EC 2.6.1.76 diaminobutyrate—2-oxoglutarate transaminase
EC 2.6.1.77 taurine—pyruvate aminotransferase
EC 2.6.1.78 aspartate—prephenate aminotransferase
EC 2.6.1.79 glutamate—prephenate aminotransferase
EC 2.6.1.80 nicotianamine aminotransferase
EC 2.6.1.81 succinylornithine transaminase
EC 2.6.1.82 putrescine—2-oxoglutarate transaminase
EC 2.6.1.83 LL-diaminopimelate aminotransferase
EC 2.6.1.84 arginine—pyruvate transaminase
EC 2.6.1.85 aminodeoxychorismate synthase
EC 2.6.1.86 2-amino-4-deoxychorismate synthase
EC 2.6.1.87 UDP-4-amino-4-deoxy-L-arabinose aminotransferase
EC 2.6.1.88 methionine transaminase
EC 2.6.1.89 dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose transaminase
EC 2.6.1.90 dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose transaminase
EC 2.6.1.91 deleted identical to EC 2.6.1.34
EC 2.6.1.92 UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine transaminase
EC 2.6.1.93 neamine transaminase
EC 2.6.1.94 2'-deamino-2'-hydroxyneamine transaminase
EC 2.6.1.95 neomycin C transaminase
EC 2.6.1.96 4-aminobutyrate—pyruvate transaminase
EC 2.6.1.97 archaeosine synthase
EC 2.6.1.98 UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
EC 2.6.1.99 L-tryptophan—pyruvate aminotransferase
EC 2.6.1.100 L-glutamine:2-deoxy-scyllo-inosose aminotransferase
EC 2.6.1.101 L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
EC 2.6.1.102 GDP-perosamine synthase
EC 2.6.1.103 (S)-3,5-dihydroxyphenylglycine transaminase
EC 2.6.1.104 3-dehydro-glucose-6-phosphate—glutamate transaminase
EC 2.6.1.105 lysine—8-amino-7-oxononanoate transaminase
EC 2.6.1.106 dTDP-3-amino-3,4,6-trideoxy-α-D-glucose transaminase
EC 2.6.1.107 β-methylphenylalanine transaminase
EC 2.6.1.108 (5-formylfuran-3-yl)methyl phosphate transaminase
EC 2.6.1.109 8-amino-3,8-dideoxy-α-D-manno-octulosonate transaminase
EC 2.6.1.110 dTDP-4-dehydro-2,3,6-trideoxy-D-glucose 4-aminotransferase
EC 2.6.1.111 3-aminobutanoyl-CoA transaminase
EC 2.6.1.112 (S)-ureidoglycine—glyoxylate transaminase
EC 2.6.1.113 putrescine—pyruvate transaminase
EC 2.6.1.114 8-demethyl-8-aminoriboflavin-5′-phosphate synthase

Entries

EC 2.6.1.51

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.

[EC 2.6.1.51 created 1972]

EC 2.6.1.52

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-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli [2,3]. It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in Escherichia coli (using Reaction 2 above) [3]. In Escherichia coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4].

Links to other databases: BRENDA, EXPASY, GTD, KEGG, 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 2.6.1.52 created 1972, modified 2006]

[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)]

EC 2.6.1.54

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.

[EC 2.6.1.54 created 1976]

EC 2.6.1.55

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]

[EC 2.6.1.55 created 1976, modified 2003]

EC 2.6.1.56

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]

[EC 2.6.1.56 created 1976]

EC 2.6.1.57

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]

[EC 2.6.1.57 created 1976]

EC 2.6.1.58

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]

[EC 2.6.1.58 created 1978]

EC 2.6.1.59

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, 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]

[EC 2.6.1.59 created 1978]

EC 2.6.1.60

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 2.6.1.60 created 1978]

[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)]

EC 2.6.1.62

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.

[EC 2.6.1.62 created 1983]

EC 2.6.1.63

Accepted name: kynurenine—glyoxylate transaminase

Reaction: L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine

For diagram click here (mechanism).

Other name(s): kynurenine-glyoxylate aminotransferase

Systematic name: L-kynurenine:glyoxylate aminotransferase (cyclizing)

Comments: Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 74506-33-5

References:

1. Harada, I. [Glucagen inducible kynurenine aminotransferase.] Wakayama Igaku 31 (1980) 61-68. (in Japanese)

[EC 2.6.1.63 created 1983]

EC 2.6.1.64

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]

[EC 2.6.1.64 created 1984]

EC 2.6.1.65

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]

[EC 2.6.1.65 created 1984]

EC 2.6.1.66

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.

[EC 2.6.1.66 created 1984]

EC 2.6.1.67

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 2.6.1.67 created 1989]

[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)]

EC 2.6.1.70

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.

[EC 2.6.1.70 created 1989]

EC 2.6.1.71

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.

[EC 2.6.1.71 created 1990]

EC 2.6.1.72

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, 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.

[EC 2.6.1.72 created 1990]

EC 2.6.1.73

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, 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.

[EC 2.6.1.73 created 1992]

EC 2.6.1.74

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]

[EC 2.6.1.74 created 1992, modified 2005]

EC 2.6.1.75

Accepted name: cysteine-conjugate transaminase

Reaction: S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate = S-(4-bromophenyl)mercaptopyruvate + L-glutamate

For diagram click here (mechanism).

Other name(s): cysteine conjugate aminotransferase; cysteine-conjugate α-ketoglutarate transaminase (CAT-1)

Systematic name: S-(4-bromophenyl)-L-cysteine:2-oxoglutarate aminotransferase

Comments: A number of cysteine conjugates can also act.

Links to other databases: BRENDA, EXPASY, KEGG, 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]

[EC 2.6.1.75 created 1992]

EC 2.6.1.76

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, 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]

[EC 2.6.1.76 created 2000, modified 2006]

EC 2.6.1.77

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]

[EC 2.6.1.77 created 2003]

EC 2.6.1.78

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, 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]

[EC 2.6.1.78 created 2005]

EC 2.6.1.79

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, 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]

[EC 2.6.1.79 created 2005]

EC 2.6.1.80

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]

[EC 2.6.1.80 created 2005]

EC 2.6.1.81

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, 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]

[EC 2.6.1.81 created 2006]

EC 2.6.1.82

Accepted name: putrescine—2-oxoglutarate transaminase

Reaction: putrescine + 2-oxoglutarate = 1-pyrroline + L-glutamate + H2O (overall reaction)
(1a) putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
(1b) 4-aminobutanal = 1-pyrroline + H2O (spontaneous)

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; putrescine:2-oxoglutarate aminotransferase; putrescine transaminase (ambiguous); putrescine aminotransferase (ambiguous)

Systematic name: butane-1,4-diamine:2-oxoglutarate aminotransferase

Comments: A pyridoxal-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which is a substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine—pyruvate transaminase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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]

[EC 2.6.1.82 created 2006, modified 2017]

EC 2.6.1.83

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]

[EC 2.6.1.83 created 2006]

EC 2.6.1.84

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]

[EC 2.6.1.84 created 2007]

EC 2.6.1.85

Accepted name: aminodeoxychorismate synthase

Reaction: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate

For diagram click here.

Other name(s): ADC synthase; 4-amino-4-deoxychorismate synthase; PabB; chorismate:L-glutamine amido-ligase (incorrect)

Systematic name: chorismate:L-glutamine aminotransferase

Comments: The enzyme is composed of two parts, PabA and PabB. In the absence of PabA and glutamine, PabB converts ammonia and chorismate into 4-amino-4-deoxychorismate (in the presence of Mg2+). PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. This enzyme is coupled with 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate.

Links to other databases: BRENDA, EXPASY, KEGG, 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]

[EC 2.6.1.85 created 2003 as EC 6.3.5.8, transferred 2007 to EC 2.6.1.85]

EC 2.6.1.86

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]

[EC 2.6.1.86 created 2008]

EC 2.6.1.87

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]

[EC 2.6.1.87 created 2010]

EC 2.6.1.88

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]

[EC 2.6.1.88 created 2011]

EC 2.6.1.89

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]

[EC 2.6.1.89 created 2011]

EC 2.6.1.90

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 2.6.1.90 created 2011]

[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)]

EC 2.6.1.92

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, 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]

[EC 2.6.1.92 created 2011, modified 2018]

EC 2.6.1.93

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, 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]

[EC 2.6.1.93 created 2012]

EC 2.6.1.94

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]

[EC 2.6.1.94 created 2012]

EC 2.6.1.95

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, 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]

[EC 2.6.1.95 created 2012]

EC 2.6.1.96

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; 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]

[EC 2.6.1.96 created 2012]

EC 2.6.1.97

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]

[EC 2.6.1.97 created 2012]

EC 2.6.1.98

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, 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]

[EC 2.6.1.98 created 2012]

EC 2.6.1.99

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, 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]

[EC 2.6.1.99 created 2012]

EC 2.6.1.100

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, 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]

[EC 2.6.1.100 created 2013]

EC 2.6.1.101

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, 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]

[EC 2.6.1.101 created 2013]

EC 2.6.1.102

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, 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]

[EC 2.6.1.102 created 2013]

EC 2.6.1.103

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.

[EC 2.6.1.103 created 2013]

EC 2.6.1.104

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, 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]

[EC 2.6.1.104 created 2014]

EC 2.6.1.105

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, 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]

[EC 2.6.1.105 created 2014]

EC 2.6.1.106

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, 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]

[EC 2.6.1.106 created 2014]

EC 2.6.1.107

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, 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]

[EC 2.6.1.107 created 2014]

EC 2.6.1.108

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]

[EC 2.6.1.108 created 2015]

EC 2.6.1.109

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, 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]

[EC 2.6.1.109 created 2015]

EC 2.6.1.110

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]

[EC 2.6.1.110 created 2016]

EC 2.6.1.111

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]

[EC 2.6.1.111 created 2017]

EC 2.6.1.112

Accepted name: (S)-ureidoglycine—glyoxylate transaminase

Reaction: (S)-ureidoglycine + glyoxylate = N-carbamoyl-2-oxoglycine + 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, 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]

[EC 2.6.1.112 created 2017]

EC 2.6.1.113

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]

[EC 2.6.1.113 created 2017]

EC 2.6.1.114

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, 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]

[EC 2.6.1.114 created 2018]


Continued with EC 2.6.3 and EC 2.6.99
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