EC number:3.1.3.89

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.89
Description:5'-deoxynucleotidase.
Cath: 1.10.3210.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.89
BRENDA Enzyme Link: BRENDA 3.1.3.89
KEGG Enzyme Link: KEGG3.1.3.89
BioCyc Enzyme Link: BioCyc 3.1.3.89
ExPASy Enzyme Link: ExPASy3.1.3.89
EC2PDB Enzyme Link: EC2PDB 3.1.3.89
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.89
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.89
IntEnz Enzyme Link: IntEnz 3.1.3.89
MEDLINE Enzyme Link: MEDLINE 3.1.3.89

EC number:3.1.3.89

MSA:

3.1.3.89;
Phylogenetic Tree:

3.1.3.89;
Uniprot:
M-CSA:
RHEA:36167 a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + 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
General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG.Proudfoot M, Kuznetsova E, Brown G, Rao NN, Kitagawa M, Mori H, Savchenko A, Yakunin AF2004 Dec 2415489502
Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli.Zimmerman MD, Proudfoot M, Yakunin A, Minor W2008 Apr 1818353368