L-lysine 6-transaminase
| L-lysine 6-transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.36 | ||||||||
| CAS no. | 9054-68-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
L-lysine 6-transaminase (EC 2.6.1.36) is an enzyme originally characterised from Flavobacterium fuscum that catalyzes a reversible chemical reaction that interconverts L-lysine and α-ketoglutaric acid with L-allysine and glutamic acid.[1][2]
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. This enzyme participates in lysine biosynthesis. It uses pyridoxal phosphate as a cofactor.[3]
Nomenclature
The systematic name of this enzyme class is L-lysine:2-oxoglutarate 6-aminotransferase. Other names in common use include
- lysine 6-aminotransferase,
- lysine epsilon-aminotransferase,
- lysine epsilon-transaminase,
- lysine:2-ketoglutarate 6-aminotransferase,
- L-lysine-alpha-ketoglutarate aminotransferase, and
- L-lysine-alpha-ketoglutarate 6-aminotransferase.[3]
Structure
L-lysine 6-transaminase belongs to the aminotransferase class-III family.[4] Crystal structures of L-lysine 6-transaminase reveal a Glu243 “switch” through which the enzyme changes substrate specificities.[5]
References
- ↑ Soda K, Misono H, Yamamoto T (1968). "L-Lysine:alpha-ketoglutarate aminotransferase. I. Identification of a product, delta-1-piperideine-6-carboxylic acid". Biochemistry. 7 (11): 4102–9. doi:10.1021/bi00851a045. PMID 5722275.
- ↑ Soda K, Misono H (1968). "L-Lysine:alpha-ketoglutarate aminotransferase. II. Purification, crystallization, and properties". Biochemistry. 7 (11): 4110–9. doi:10.1021/bi00851a046. PMID 5722276.
- 1 2 Enzyme 2.6.1.36 at KEGG Pathway Database.
- ↑ Pfam PF00202
- ↑ Mani Tripathi S, Ramachandran R (2006). "Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine epsilon-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv". Journal of Molecular Biology. 362 (5): 877–86. doi:10.1016/j.jmb.2006.08.019. PMID 16950391.