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 |
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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 |