KEGG   ENZYME: 2.6.1.126
Entry
EC 2.6.1.126                Enzyme                                 
Name
L-aspartate:5-guanidino-3-methyl-2-oxopentanoate transaminase;
argM (gene name);
mrsB (gene name)
Class
Transferases;
Transferring nitrogenous groups;
Transaminases
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)
R13306
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
Reference
1  [PMID:20190091]
  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
Appl Environ Microbiol 76:2500-8 (2010)
DOI:10.1128/AEM.00666-09
  Sequence
[psb:Psyr_0117]
Reference
2  [PMID:24907335]
  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
Appl Environ Microbiol 80:5021-7 (2014)
DOI:10.1128/AEM.01172-14
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.6.1.126
IUBMB Enzyme Nomenclature: 2.6.1.126
ExPASy - ENZYME nomenclature database: 2.6.1.126
BRENDA, the Enzyme Database: 2.6.1.126
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