EC 22.214.171.124 - 5'-deoxynucleotidase
IntEnz Enzyme Nomenclature
- a 2'-deoxyribonucleoside 5'-monophosphate + H2O = a 2'-deoxyribonucleoside + phosphate
The enzyme, characterized from the bacterium Escherichia coli, shows strict specificity towards deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates. A divalent metal cation is required for activity, with cobalt providing the highest activity.
Links to other databases
General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG.J. Biol. Chem. 279 : 54687-54694 (2004). [PMID: 15489502]
Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli.J. Mol. Biol. 378 : 215-226 (2008). [PMID: 18353368]
[EC 126.96.36.199 created 2013]