The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: 5′-deoxynucleotidase
Reaction: a 2′-deoxyribonucleoside 5′-monophosphate + H2O = a 2′-deoxyribonucleoside + phosphate
Other name(s): yfbR (gene name)
Systematic name: 2′-deoxyribonucleoside 5′-monophosphate phosphohydrolase
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N.N., Kitagawa, M., Mori, H., Savchenko, A. and Yakunin, A.F. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. J. Biol. Chem. 279 (2004) 54687–54694. [DOI] [PMID: 15489502]
2.  Zimmerman, M.D., Proudfoot, M., Yakunin, A. and 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 (2008) 215–226. [DOI] [PMID: 18353368]
[EC created 2013]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald