|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
acid phosphatase / phosphotransferase: aphA
CPS-53 (KpLE1) prophage; deoxyribonucleoside 5'-monophosphate phosphatase: yfdR
dCMP phosphohydrolase: yfbR
Reaction Locations: periplasm (sensu Gram-negative Bacteria), cytosol
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: Balanced.
dGMP + H2O → 2'-deoxyguanosine + phosphate (184.108.40.206)
dAMP + H2O → 2'-deoxyadenosine + phosphate (220.127.116.11)
dUMP + H2O → 2'-deoxyuridine + phosphate (18.104.22.168)
dCMP + H2O → 2'-deoxycytidine + phosphate (22.214.171.124)
dTMP + H2O → thymidine + phosphate (126.96.36.199)
Enzyme Commission Primary Name: 5′-deoxynucleotidase
Enzyme Commission Synonyms: yfbR (gene name)
Enzyme Commission Summary:
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.
Proudfoot04: Proudfoot M, Kuznetsova E, Brown G, Rao NN, Kitagawa M, Mori H, Savchenko A, Yakunin AF (2004). "General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG." J Biol Chem 279(52);54687-94. PMID: 15489502
Zimmerman08: Zimmerman MD, Proudfoot M, Yakunin A, Minor W (2008). "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(1);215-26. PMID: 18353368
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