Glutamine—phenylpyruvate transaminase
| glutamine-phenylpyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.64 | ||||||||
| CAS no. | 68518-06-9 | ||||||||
| 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-phenylpyruvate transaminase (EC 2.6.1.64) is an enzyme that catalyzes the chemical reaction
- L-glutamine + phenylpyruvate 2-oxoglutaramate + L-phenylalanine
Thus, the two substrates of this enzyme are L-glutamine and phenylpyruvate, whereas its two products are 2-oxoglutaramate and L-phenylalanine.
This enzyme belongs to the family of transferases, to be specific, the transaminases, that transfer nitrogenous groups. The systematic name of this enzyme class is L-glutamine:phenylpyruvate aminotransferase. Other names in common use include glutamine transaminase K, and glutamine-phenylpyruvate aminotransferase. It employs one cofactor, pyridoxal phosphate.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1YIY and 1YIZ.
References
[edit]- Cooper AJ (1978). "Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L-phenylalanine and alpha-keto-gamma-methiolbutyrate". Anal. Biochem. 89 (2): 451–60. doi:10.1016/0003-2697(78)90374-3. PMID 727444.
- Cooper AJ, Meister A (1974). "Isolation and properties of a new glutamine transaminase from rat kidney". J. Biol. Chem. 249 (8): 2554–61. doi:10.1016/S0021-9258(19)42765-8. PMID 4822504.
