| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
| ID: | 3.1.3.63 |
|---|---|
| Description: | 2-carboxy-D-arabinitol-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 3.1.3.63 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.63 |
| KEGG Enzyme Link: | KEGG3.1.3.63 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.63 |
| ExPASy Enzyme Link: | ExPASy3.1.3.63 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.63 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.63 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.63 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.63 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.63 |
| RHEA:17837 | 2-carboxy-D-arabinitol 1-phosphate + H2O = 2-carboxy-D-arabinitol + 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 |
|---|---|---|---|
| The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. | Schnurr K, Belkner J, Ursini F, Schewe T, Kühn H | 1996 Mar 1 | 8617728 |
| The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. | Ursini F, Maiorino M, Gregolin C | 1985 Mar 29 | 3978121 |