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2.6.1.107 |
Description |
beta-methylphenylalanine transaminase |
Alternative names |
(2S,3S)-3-methylphenylalanine:2-oxoglutarate aminotransferase;
TyrB; |
Catalyzed reaction |
(2S,3S)-3-methylphenylalanine + 2-oxoglutarate =
(3S)-2-oxo-3-phenylbutanoate + L-glutamate
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Cofactor |
Pyridoxal-phosphate. |
Comments |
Requires pyridoxal phosphate. Isolated from the bacterium
Streptomyces hygroscopicus NRRL3085. It is involved in the biosynthesis of the glycopeptide antibiotic mannopeptimycin.
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The only functionally validated enzyme with this activity, is TyrB from E. coli, an aromatic-aminoacid-transferase included in family 2.7.1.57_a.
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Organisms |
-Eubacteria |
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Links |
Enzyme (activities) 2.6.1.107
BRENDA (activities) 2.6.1.107
KEGG (pathways) 2.6.1.107
PLPMDB (PLP mutants) 2.6.1.107
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References |
Huang YT, Lyu SY, Chuang PH, Hsu NS, Li YS, Chan HC, Huang CJ, Liu YC, Wu CJ, Yang WB, Li TL (2009) In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-beta-methylphenylalanine in glycopeptide antibiotic mannopeptimycin Chembiochem 10 2480-7. Articles on 2.6.1.107 |
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last changed |
2019/03/25 11:14 |
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