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

IUBMB entry for 3.5.2.11
BRENDA references for 3.5.2.11 (Recommended.)
PubMed references for 3.5.2.11
PubMed Central references for 3.5.2.11
Google Scholar references for 3.5.2.11
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: 298–300. doi:10.1016/0014-5793(78)80240-3. PMID 26602.
Shvyadas VK, Galaev IYu and Kozlova EV (Moscow). "Preparation and characterization of L-alpha-aminocaprolactam hydrolase from cells of Cryptococcus laurentii". B Biochemistry: 1268–1273.