Glutamine-pyruvate transaminase

From Wikipedia, the free encyclopedia

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

L-glutamine + pyruvate $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 2.6.1.15
BRENDA references for 2.6.1.15 (Recommended.)
PubMed references for 2.6.1.15
PubMed Central references for 2.6.1.15
Google Scholar references for 2.6.1.15
Cooper JL, Meister A (1972). "Isolation and properties of highly purified glutamine transaminase". Biochemistry. 11: 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: 17–35. PMID 13201566.