Diamine transaminase
| diamine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.29 | ||||||||
| CAS no. | 9031-83-8 | ||||||||
| 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 diamine transaminase (EC 2.6.1.29) is an enzyme that catalyzes the chemical reaction
- an alpha,omega-diamine + 2-oxoglutarate an omega-aminoaldehyde + L-glutamate
Thus, the two substrates of this enzyme are alpha,omega-diamine and 2-oxoglutarate, whereas its two products are omega-aminoaldehyde 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 diamine:2-oxoglutarate aminotransferase. Other names in common use include amine transaminase, amine-ketoacid transaminase, diamine aminotransferase, and diamine-ketoglutaric transaminase. This enzyme participates in urea cycle and metabolism of amino groups.
References
- Kim K (1964). "Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli". J. Biol. Chem. 239: 783–786.