EC number:3.5.1.74
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.74 |
|---|---|
| Description: | Chenodeoxycholoyltaurine hydrolase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.74 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.74 |
| KEGG Enzyme Link: | KEGG3.5.1.74 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.74 |
| ExPASy Enzyme Link: | ExPASy3.5.1.74 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.74 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.74 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.74 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.74 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.74 |
| RHEA:16309 | H2O + taurochenodeoxycholate = chenodeoxycholate + taurine |
| 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 |
|---|---|---|---|
| Bile salt hydrolase of Bifidobacterium longum-biochemical and genetic characterization. | Tanaka H, Hashiba H, Kok J, Mierau I | 2000 Jun | 10831430 |
| The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. | O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE | 2003 Sep 5 | 12810727 |