Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases

2'-deoxyribonucleoside 5'-monophosphate phosphohydrolase

a 2'-deoxyribonucleoside 5'-monophosphate + H2O = a 2'-deoxyribonucleoside + phosphate [RN:R10776]

R10776 > R01569 R01664 R01968 R02088 R02102

2'-deoxyribonucleoside 5'-monophosphate [CPD:C00676];
H2O [CPD:C00001]

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.

EC 3.1.3.89 created 2013

1  [PMID:15489502]

Proudfoot M, Kuznetsova E, Brown G, Rao NN, Kitagawa M, Mori H, Savchenko A, Yakunin AF

General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG.

J Biol Chem 279:54687-94 (2004)
DOI:10.1074/jbc.M411023200

[eco:b2291]

2  [PMID:18353368]

Zimmerman MD, Proudfoot M, Yakunin A, Minor W

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 378:215-26 (2008)
DOI:10.1016/j.jmb.2008.02.036

[eco:b2291]