| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.62 |
|---|---|
| Description: | Acetylputrescine deacetylase. |
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 3.5.1.62 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.62 |
| KEGG Enzyme Link: | KEGG3.5.1.62 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.62 |
| ExPASy Enzyme Link: | ExPASy3.5.1.62 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.62 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.62 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.62 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.62 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.62 |
| RHEA:23412 | H2O + N-acetylputrescine = acetate + putrescine |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme. | Sakurada K, Ohta T, Fujishiro K, Hasegawa M, Aisaka K | 1996 Oct | 8824626 |
| Crystallization and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata. | Fujishiro K, Ando M, Uwajima T | 1988 Dec 30 | 3207420 |
| Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa. | Krämer A, Herzer J, Overhage J, Meyer-Almes FJ | 2016 Mar 9 | 26956223 |