Glutamine—pyruvate transaminase
| glutamine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.15 | ||||||||
| CAS no. | 9030-44-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
