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2.6.1.84 |
Description |
Arginine--pyruvate transaminase |
Alternative names |
arginine:pyruvate aminotransferase; AruH. |
Catalyzed reaction |
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine. |
Cofactor |
Pyridoxal-phosphate. |
Comments |
A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked. |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.6.1.84
BRENDA (activities) 2.6.1.84
KEGG (pathways) 2.6.1.84
PLPMDB (PLP mutants) 2.6.1.84
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References |
Articles on 2.6.1.84 |
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last changed |
2017/10/10 14:10 |
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