| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.24 |
|---|---|
| Description: | Choloylglycine hydrolase. |
| Alternative Name: |
Glycocholase. Bile salt hydrolase. |
| Cath: | 3.60.60.10; |
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 3.5.1.24 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.24 |
| KEGG Enzyme Link: | KEGG3.5.1.24 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.24 |
| ExPASy Enzyme Link: | ExPASy3.5.1.24 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.24 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.24 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.24 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.24 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.24 |
| RHEA:19353 | glycocholate + H2O = cholate + glycine |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens. | Coleman JP, Hudson LL | 1995 Jul | 7618863 |
| Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product. | Rossocha M, Schultz-Heienbrok R, von Moeller H, Coleman JP, Saenger W | 2005 Apr 19 | 15823032 |
| Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay. | Christiaens H, Leer RJ, Pouwels PH, Verstraete W | 1992 Dec | 1476424 |
| Bile salt hydrolase of Bifidobacterium longum-biochemical and genetic characterization. | Tanaka H, Hashiba H, Kok J, Mierau I | 2000 Jun | 10831430 |