Biology:Glutamine—phenylpyruvate transaminase
From HandWiki
| glutamine-phenylpyruvate transaminase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.6.1.64 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a glutamine-phenylpyruvate transaminase (EC 2.6.1.64) is an enzyme that catalyzes the chemical reaction
- L-glutamine + phenylpyruvate [math]\displaystyle{ \rightleftharpoons }[/math] 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
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1YIY and 1YIZ.
References
- 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.
- "Isolation and properties of a new glutamine transaminase from rat kidney". J. Biol. Chem. 249 (8): 2554–61. 1974. PMID 4822504.
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