| L-lysine-lactamase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.2.11 | ||||||||
| CAS no. | 52652-61-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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
L-lysineThus, 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.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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