L-lysine 6-transaminase
L-lysine 6-transaminase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.6.1.36 | ||||||||
CAS no. | 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 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
[edit]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
[edit]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
[edit]- ^ 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.
Further reading
[edit]- 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.
- 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.