L-lysine-lactamase
In enzymology, a L-lysine-lactamase (EC 3.5.2.11) is an enzyme that catalyzes the chemical reaction
- L-lysine 1,6-lactam + H2O L-lysine
Thus, the two substrates of this enzyme are L-lysine 1,6-lactam and H2O, whereas its product is L-lysine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is L-lysine-1,6-lactam lactamhydrolase. Other names in common use include L-alpha-aminocaprolactam hydrolase, and L-lysinamidase.
References
- Fukumura T, Talbot G, Misono H, Teramura Y, Kato K, Soda K (1978). "Purification and properties of a novel enzyme, L-alpha-amino-epsilon-caprolactamase from Cryptococcus laurentii". FEBS Lett. 89 (2): 298–300. doi:10.1016/0014-5793(78)80240-3. PMID 26602.
- Shvyadas, VK; Galaev, IYu; Kozlova, EV (1984). "Preparation and characterization of L-alpha-aminocaprolactam hydrolase from cells of Cryptococcus laurentii". Biochemistry (Moscow) 49: 1268–1273.
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