Jump to content

Glutamine—pyruvate transaminase

From Wikipedia, the free encyclopedia
glutamine-pyruvate transaminase
Identifiers
EC no.2.6.1.15
CAS no.9030-44-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction

L-glutamine + pyruvate 2-oxoglutaramate + L-alanine

Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutaramate 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-glutamine:pyruvate aminotransferase. Other names in common use include glutaminase II, L-glutamine transaminase L, and glutamine-oxo-acid transaminase. This enzyme participates in glutamate metabolism. It employs one cofactor, pyridoxal phosphate.

Structural studies

[edit]

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1V2D, 1V2E, and 1V2F.

References

[edit]
  • Cooper JL, Meister A (1972). "Isolation and properties of highly purified glutamine transaminase". Biochemistry. 11 (5): 661–71. doi:10.1021/bi00755a001. PMID 5059882.
  • MEISTER A (1954). "Studies on the mechanism and specificity of the glutamine-alpha-keto acid transamination-deamidation reaction". J. Biol. Chem. 210 (1): 17–35. doi:10.1016/S0021-9258(18)65429-8. PMID 13201566.