| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.2 In cyclic amides |
| ID: | 3.5.2.11 |
|---|---|
| Description: | L-lysine-lactamase. |
| Alternative Name: |
L-lysinamidase. L-alpha-aminocaprolactam hydrolase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 3.5.2.11 |
| BRENDA Enzyme Link: | BRENDA 3.5.2.11 |
| KEGG Enzyme Link: | KEGG3.5.2.11 |
| BioCyc Enzyme Link: | BioCyc 3.5.2.11 |
| ExPASy Enzyme Link: | ExPASy3.5.2.11 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.2.11 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.2.11 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.2.11 |
| IntEnz Enzyme Link: | IntEnz 3.5.2.11 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.2.11 |
| RHEA:21388 | H2O + L-2-aminohexano-6-lactam = L-lysine |
| RULE(radius=1) | ([*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6])>>[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1].[OH2;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and properties of a novel enzyme, L-alpha-amino-epsilon-caprolactamase from Cryptococcus laurentii. | Fukumura T, Talbot G, Misono H, Teramura Y, Kato K, Soda K | 1978 May 15 | 26602 |