In enzymology, a glutamine-phenylpyruvate transaminase (EC 2.6.1.64) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
- 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. PMID 4822504.
