Entry Name L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase;
Class Transferases;BRITE hierarchy
Sysname L-aspartate:5-guanidino-3-methyl-2-oxopentanoate aminotransferase
Reaction(IUBMB) L-aspartate + (3R)-5-guanidino-3-methyl-2-oxopentanoate = oxaloacetate + (3R)-3-methyl-L-arginine [RN:
R13306 ]
Reaction(KEGG) Substrate L-aspartate [CPD:
C00049 ];
(3R)-5-guanidino-3-methyl-2-oxopentanoate [CPD:
C20234 ]
Product oxaloacetate [CPD:
C00036 ];
(3R)-3-methyl-L-arginine [CPD:
C22904 ]
Comment 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.
History EC 2.6.1.126 created 2024
Orthology K27543 L-arginine:2-oxoglutarate/L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase
Genes Taxonomy Reference Authors Braun SD, Hofmann J, Wensing A, Ullrich MS, Weingart H, Volksch B, Spiteller D
Title Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93.
Journal Sequence Reference Authors Feng J, Wu J, Gao J, Xia Z, Deng Z, He X.
Title Biosynthesis of the beta-methylarginine residue of peptidyl nucleoside arginomycin in Streptomyces arginensis NRRL 15941.
Journal Sequence Other DBs ExPASy - ENZYME nomenclature database: 2.6.1.126
LinkDB All DBs
