Arginine—pyruvate transaminase

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
Arginine-pyruvate transaminase
Identifiers
EC no.2.6.1.84
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

    • 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.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.