Biology:L-lysine 6-transaminase
| L-lysine 6-transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.36 | ||||||||
| CAS number | 9054-68-6 | ||||||||
| 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 L-lysine 6-transaminase (EC 2.6.1.36) is an enzyme that catalyzes the chemical reaction
- L-lysine + 2-oxoglutarate [math]\displaystyle{ \rightleftharpoons }[/math] 2-aminoadipate 6-semialdehyde + L-glutamate
Thus, the two substrates of this enzyme are L-lysine and 2-oxoglutarate, whereas its two products are 2-aminoadipate 6-semialdehyde and L-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. This enzyme participates in lysine biosynthesis. It employs one cofactor, pyridoxal phosphate.
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.
Structure
L-lysine 6-transaminase belongs to the aminotransferase class-III family.[1] Crystal structures of L-lysine 6-transaminase reveal a Glu243 “switch” through which the enzyme changes substrate specificities.[2]
References
Further reading
- "L-Lysine:alpha-ketoglutarate aminotransferase. I. Identification of a product, delta-1-piperideine-6-carboxylic acid". Biochemistry 7 (11): 4102–9. 1968. doi:10.1021/bi00851a045. PMID 5722275.
- "L-Lysine:alpha-ketoglutarate aminotransferase. II. Purification, crystallization, and properties". Biochemistry 7 (11): 4110–9. 1968. doi:10.1021/bi00851a046. PMID 5722276.
- Tripathi, Sarvind; Ramachandran, Ravishankar (2006). "Direct Evidence for a Glutamate Switch Necessary for Substrate Recognition: Crystal Structures of Lysine ε-Aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv". Journal of Molecular Biology 362 (5): 877–886. doi:10.1016/j.jmb.2006.08.019. PMID 16950391.
 |  |
