Biology:Arginine—pyruvate transaminase
From HandWiki
Arginine-pyruvate transaminase | |||||||||
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Identifiers | |||||||||
EC number | 2.6.1.84 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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.
References
- "Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1". J. Bacteriol. 189 (11): 3954–9. 2007. doi:10.1128/JB.00262-07. PMID 17416668.
- "Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa". J. Bacteriol. 189 (11): 3945–53. 2007. doi:10.1128/JB.00261-07. PMID 17416670.
Original source: https://en.wikipedia.org/wiki/Arginine—pyruvate transaminase.
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