| EC |
2.6.1.84 |
| Accepted name: |
arginine—pyruvate transaminase |
| Reaction: |
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine |
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For diagram of arginine-catabolism pathway, click here |
| Other name(s): |
arginine:pyruvate transaminase; AruH; ATase |
| Systematic name: |
L-arginine:pyruvate aminotransferase |
| 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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Yang, Z. and Lu, C.-D. Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1. J. Bacteriol. 189 (2007) 3954–3959. [DOI] [PMID: 17416668] |
| 2. |
Yang, Z. and Lu, C.D. Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa. J. Bacteriol. 189 (2007) 3945–3953. [DOI] [PMID: 17416670] |
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| [EC 2.6.1.84 created 2007] |
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