| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
| ID: | 3.1.3.22 |
|---|---|
| Description: | Mannitol-1-phosphatase. |
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 3.1.3.22 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.22 |
| KEGG Enzyme Link: | KEGG3.1.3.22 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.22 |
| ExPASy Enzyme Link: | ExPASy3.1.3.22 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.22 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.22 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.22 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.22 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.22 |
| RHEA:19537 | D-mannitol 1-phosphate + H2O = D-mannitol + 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Molecular cloning and functional expression of mannitol-1-phosphatase from the apicomplexan parasite Eimeria tenella. | Liberator P, Anderson J, Feiglin M, Sardana M, Griffin P, Schmatz D, Myers RW | 1998 Feb 13 | 9461622 |
| Enzymatic studies on mannitol formation by Piricularia oryzae. | YAMADA H, OKAMOTO K, KODAMA K, NOGUCHI F, TANAKA S | 1961 May | 13787089 |
| A pathway for photosynthetic carbon flow to mannitol in celery leaves : activity and localization of key enzymes. | Rumpho ME, Edwards GE, Loescher WH | 1983 Dec | 16663332 |