The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 3.1.3.89     
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
References:
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. [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. [PMID: 18353368]
[EC 3.1.3.89 created 2013]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald