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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a L-lysine 6-transaminase (EC 2.6.1.36) is an enzyme that catalyzes the chemical reaction

L-lysine + 2-oxoglutarate ${\displaystyle \rightleftharpoons }$ 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

1. Pfam PF00202
2. 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

• 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.