EC number:3.5.1.60
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.60 |
|---|---|
| Description: | N-(long-chain-acyl)ethanolamine deacylase. |
| Alternative Name: |
N-acylethanolamine amidohydrolase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.60 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.60 |
| KEGG Enzyme Link: | KEGG3.5.1.60 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.60 |
| ExPASy Enzyme Link: | ExPASy3.5.1.60 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.60 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.60 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.60 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.60 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.60 |
| RHEA:17505 | H2O + N-(long-chain fatty acyl)ethanolamine = a long-chain fatty acid + ethanolamine |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Properties of rat liver N-acylethanolamine amidohydrolase. | Schmid PC, Zuzarte-Augustin ML, Schmid HH | 1985 Nov 15 | 4055775 |