| EC |
2.6.1.125 |
| 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 |
| 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. [DOI] [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. [DOI] [PMID: 24907335] |
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| [EC 2.6.1.125 created 2024] |
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