The Enzyme Database

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EC 3.5.2.11     
Accepted name: L-lysine-lactamase
Reaction: (S)-2-aminohexano-6-lactam + H2O = L-lysine
Glossary: (S)-2-aminohexano-6-lactam = L-lysine 1,6-lactam
Other name(s): L-α-aminocaprolactam hydrolase; L-lysinamidase; L-lysine-1,6-lactam lactamhydrolase
Systematic name: (S)-2-aminohexano-6-lactam lactamhydrolase
Comments: Also hydrolyses L-lysinamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52652-61-6
References:
1.  Fukumura, T., Talbot, G., Misono, H., Teremura, Y., Kato, K. and Soda, K. Purification and properties of a novel enzyme, L- α-amino-ε-caprolactamase from Cryptococcus laurentii. FEBS Lett. 89 (1978) 298–300. [DOI] [PMID: 26602]
2.  Shvyadas, V.K., Galaev, I.Yu. and Kozlova, E.V. Preparation and characterization of L-α-aminocaprolactam hydrolase from cells of Cryptococcus laurentii. Biochemistry (Moscow) 49 (1984) 1268–1273.
[EC 3.5.2.11 created 1981, modified 1989]
 
 
EC 5.1.1.15     
Accepted name: 2-aminohexano-6-lactam racemase
Reaction: (S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
Glossary: (S)-2-aminohexano-6-lactam = L-lysine 1,6-lactam
Other name(s): α-amino-ε-caprolactam racemase
Systematic name: 2-aminohexano-6-lactam racemase
Comments: Contains pyridoxal 5′-phosphate. Also racemises 2-aminopentano-5-lactam (α-amino-δ-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4). It does not catalyse the racemisation of α-amino acids but has some transaminase activity with them.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52652-64-9
References:
1.  Ahmed, S.A., Esaki, N., Tanaka, H., Soda, K. L-α-Amino-β-thio-ε-caprolactam, a new sulfur-containing substrate for α-amino-ε-caprolactam racemase. FEBS Lett. 174 (1984) 76–79.
2.  Ahmed, S.A., Esaki, N., Tanaka, H., Soda, K. Mechanism of α-amino-ε-caprolactam racemase reaction. Biochemistry 25 (1986) 385–388. [PMID: 3955003]
3.  Okazaki, S., Suzuki, A., Mizushima, T., Kawano, T., Komeda, H., Asano, Y. and Yamane, T. The novel structure of a pyridoxal 5′-phosphate-dependent fold-type I racemase, α-amino-ε-caprolactam racemase from Achromobacter obae. Biochemistry 48 (2009) 941–950. [DOI] [PMID: 19146406]
[EC 5.1.1.15 created 1999]
 
 


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