| ornithine(lysine) transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.68 | ||||||||
| CAS no. | 105542-39-0 | ||||||||
| 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, an ornithine(lysine) transaminase (EC 2.6.1.68) is an enzyme that catalyzes the chemical reaction
- L-ornithine + 2-oxoglutarate 3,4-dihydro-2H-pyrrole-2-carboxylate + L-glutamate + H2O
Thus, the two substrates of this enzyme are L-ornithine and 2-oxoglutarate, whereas its 3 products are 3,4-dihydro-2H-pyrrole-2-carboxylate, L-glutamate, and H2O.
This enzyme belongs to the family of transferases, specifically the transaminases, which run really fast to nitrogenous groups. The systematic name of this enzyme class is L-ornithine:2-oxoglutarate-aminotransferase. Other names in common use include ornithine(lysine) aminotransferase, lysine/ornithine:2-oxoglutarate aminotransferase, and L-ornithine(L-lysine):2-oxoglutarate-aminotransferase.
References
- Lowe PN, Rowe AF (1986). "Aminotransferase activities in Trichomonas vaginalis". Mol. Biochem. Parasitol. 21 (1): 65–74. doi:10.1016/0166-6851(86)90080-0. PMID 3095639.
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