| 2,5-diaminovalerate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.8 | ||||||||
| CAS no. | 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.
It employs one cofactor, pyridoxal phosphate.
Nomenclature
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.
References
- Roberts E (February 1954). "Studies of transamination". Archives of Biochemistry and Biophysics. 48 (2): 395–401. doi:10.1016/0003-9861(54)90355-0. PMID 13125615.
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