| EC |
2.6.1.126 |
| 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 |
| 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. [DOI] [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. [DOI] [PMID: 24907335] |
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| [EC 2.6.1.126 created 2024] |
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