EC 3.1.3.89 - 5'-deoxynucleotidase

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IntEnz Enzyme Nomenclature
EC 3.1.3.89

Names

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

Reaction

Cofactor

Comments:

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]

References

  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 3.1.3.89 created 2013]