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Arginine—pyruvate transaminase

From Wikipedia, the free encyclopedia
Arginine-pyruvate transaminase
Identifiers
EC no.2.6.1.84
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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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.

References

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  • Yang Z, Lu CD (2007). "Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1". J. Bacteriol. 189 (11): 3954–9. doi:10.1128/JB.00262-07. PMC 1913410. PMID 17416668.
  • Yang Z, Lu CD (2007). "Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa". J. Bacteriol. 189 (11): 3945–53. doi:10.1128/JB.00261-07. PMC 1913404. PMID 17416670.