| EC Tree |
| 3. Hydrolases |
| 3.6 Acting on acid anhydrides |
| 3.6.1 In phosphorus-containing anhydrides |
| ID: | 3.6.1.20 |
|---|---|
| Description: | 5'-acylphosphoadenosine hydrolase. |
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 3.6.1.20 |
| BRENDA Enzyme Link: | BRENDA 3.6.1.20 |
| KEGG Enzyme Link: | KEGG3.6.1.20 |
| BioCyc Enzyme Link: | BioCyc 3.6.1.20 |
| ExPASy Enzyme Link: | ExPASy3.6.1.20 |
| EC2PDB Enzyme Link: | EC2PDB 3.6.1.20 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.6.1.20 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.6.1.20 |
| IntEnz Enzyme Link: | IntEnz 3.6.1.20 |
| MEDLINE Enzyme Link: | MEDLINE 3.6.1.20 |
| RHEA:16837 | 5'-acylphosphoadenosine + H2O = a carboxylate + AMP + 2 H(+) |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Isolation and characteristics of the enzyme acyl 5'-nucleotidase. | KELLERMAN GM | 1959 May | 13651188 |