2-aminoadipate transaminase
| 2-aminoadipate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.39 | ||||||||
| CAS no. | 9033-00-5 | ||||||||
| 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, 2-aminoadipate transaminase (EC 2.6.1.39) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-2-aminoadipic acid and α-Ketoglutaric acid. Its products are 2-oxoadipic acid and L-glutamic acid.[1][2]
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-2-aminoadipate:2-oxoglutarate aminotransferase. Other names in common use include alpha-aminoadipate aminotransferase, 2-aminoadipate aminotransferase, 2-aminoadipic aminotransferase, glutamic-ketoadipic transaminase, and glutamate-alpha-ketoadipate transaminase. This enzyme participates in lysine biosynthesis and lysine degradation. It employs one cofactor, pyridoxal phosphate.[3]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DTV.
References
- ^ Enzyme 2.6.1.39 at KEGG Pathway Database.
- ^ Matsuda M, Ogur M (1969). "Separation and specificity of the yeast glutamate-alpha-ketoadipate transaminase". J. Biol. Chem. 244 (12): 3352–8. doi:10.1016/S0021-9258(18)93133-9. PMID 5792664.
- ^ Voet, Donald; Voet, Judith G. (2011). Biochemistry (4th ed.). Hoboken, NJ: Wiley. pp. 1040–41. ISBN 978-0-470-91745-9.