Enzyme

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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.

3D structure

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References

External Links

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
MSA:

3.1.3.63;

Phylogenetic Tree:

3.1.3.63;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed 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 H1996 Mar 18617728
The selenoenzyme phospholipid hydroperoxide glutathione peroxidase.Ursini F, Maiorino M, Gregolin C1985 Mar 293978121