L-lysine 6-transaminase

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

L-lysine 6-transaminase
Identifiers
EC no.2.6.1.36
CAS no.9054-68-6
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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

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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

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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

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  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

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  • 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.