EC number:3.1.3.92
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
| ID: | 3.1.3.92 |
|---|---|
| Description: | Kanosamine-6-phosphate phosphatase. |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.3.92 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.92 |
| KEGG Enzyme Link: | KEGG3.1.3.92 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.92 |
| ExPASy Enzyme Link: | ExPASy3.1.3.92 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.92 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.92 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.92 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.92 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.92 |
| RHEA:37555 | D-kanosamine 6-phosphate + H2O = kanosamine + phosphate |
| RULE(radius=1) | [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A previously unrecognized kanosamine biosynthesis pathway in Bacillus subtilis. | Vetter ND, Langill DM, Anjum S, Boisvert-Martel J, Jagdhane RC, Omene E, Zheng H, van Straaten KE, Asiamah I, Krol ES, Sanders DA, Palmer DR | 2013 Apr 24 | 23586652 |