EC number:3.5.1.51
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.51 |
|---|---|
| Description: | 4-acetamidobutyryl-CoA deacetylase. |
| Alternative Name: |
Aminobutyryl-CoA thiolesterase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.51 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.51 |
| KEGG Enzyme Link: | KEGG3.5.1.51 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.51 |
| ExPASy Enzyme Link: | ExPASy3.5.1.51 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.51 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.51 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.51 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.51 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.51 |
| RHEA:22928 | 4-acetamidobutanoyl-CoA + H2O = 4-aminobutanoyl-CoA + acetate |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](=[*:4])-[*:5].[OH2;+0:6]>>[*:1]-[NH2;+0:2].[*:4]=[C;H0;+0:3](-[*:5])-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Metabolism of L-beta-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds. | Ohsugi M, Kahn J, Hensley C, Chew S, Barker HA | 1981 Jul 25 | 6788773 |