EC Tree |
3. Hydrolases |
3.1 Acting on ester bonds |
3.1.3 Phosphoric-monoester hydrolases |
ID: | 3.1.3.63 |
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Description: | 2-carboxy-D-arabinitol-1-phosphatase. |
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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 |