L-lysine 6-transaminase

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L-lysine 6-transaminase

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

L-lysine + 2-oxoglutarate

\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

^ 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.

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.

v t e Transferase: nitrogenous groups (EC 2.6)
2.6.1: Transaminases	Aspartate transaminase GOT1 GOT2 Alanine transaminase GABA transaminase Tyrosine aminotransferase Kynurenine—oxoglutarate transaminase Ornithine aminotransferase Branched-chain amino acid aminotransferase Alanine—glyoxylate transaminase AGXT
2.6.3: Oximinotransferases	Oximinotransferase
2.6.99: Other	Pyridoxine 5'-phosphate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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