EC - 5'-deoxynucleotidase

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IntEnz Enzyme Nomenclature


Accepted name:
Other name:
yfbR (gene name)
Systematic name:
2'-deoxyribonucleoside 5'-monophosphate phosphohydrolase




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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (81) [show] [UniProt]


  1. Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N. N., Kitagawa, M., Mori, H., Savchenko, A., Yakunin, A. F.
    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]
  2. Zimmerman, M. D., 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 : 215-226 (2008). [PMID: 18353368]

[EC created 2013]