2,5-diaminovalerate transaminase
| 2,5-diaminovalerate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.8 | ||||||||
| CAS number | 9030-39-1 | ||||||||
| 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 2,5-diaminovalerate transaminase (EC 2.6.1.8) is an enzyme that catalyzes the chemical reaction
- 2,5-diaminopentanoate + 2-oxoglutarate 5-amino-2-oxopentanoate + L-glutamate
Thus, the two substrates of this enzyme are 2,5-diaminopentanoate and 2-oxoglutarate, whereas its two products are 5-amino-2-oxopentanoate and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 2,5-diaminopentanoate:2-oxoglutarate aminotransferase. Other names in common use include diamino-acid transaminase, and diamino acid aminotransferase. It employs one cofactor, pyridoxal phosphate.
References
- ROBERTS E (1954). "Studies of transamination". Arch. Biochem. Biophys. 48 (2): 395&ndash, 401. doi:10.1016/0003-9861(54)90355-0. PMID 13125615.
This article is issued from
Wikipedia.
The text is licensed under Creative Commons - Attribution - Sharealike.
Additional terms may apply for the media files.