Arginine-pyruvate transaminase
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In enzymology, an arginine-pyruvate transaminase (EC 2.6.1.84) is an enzyme that catalyzes the chemical reaction
- L-arginine + pyruvate
5-guanidino-2-oxopentanoate + L-alanine
Thus, the two substrates of this enzyme are L-arginine and pyruvate, whereas its two products are 5-guanidino-2-oxopentanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arginine:pyruvate aminotransferase. Other names in common use include arginine:pyruvate transaminase, and AruH.
[edit] References
- IUBMB entry for 2.6.1.84
- BRENDA references for 2.6.1.84 (Recommended.)
- PubMed references for 2.6.1.84
- PubMed Central references for 2.6.1.84
- Google Scholar references for 2.6.1.84
- Yang Z, Lu CD (2007). "Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1". J. Bacteriol. 189: 3954–9. doi:. PMID 17416668.
- Yang Z, Lu CD (2007). "Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa". J. Bacteriol. 189: 3945–53. doi:. PMID 17416670.
[edit] External links
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