Entry |
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Name |
5'-deoxynucleotidase;
yfbR (gene name)
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Class |
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
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Sysname |
2'-deoxyribonucleoside 5'-monophosphate phosphohydrolase
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Reaction(IUBMB) |
a 2'-deoxyribonucleoside 5'-monophosphate + H2O = a 2'-deoxyribonucleoside + phosphate [RN: R10776]
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Reaction(KEGG) |
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Substrate |
2'-deoxyribonucleoside 5'-monophosphate [CPD: C00676];
H2O [CPD: C00001]
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Product |
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Comment |
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.
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History |
EC 3.1.3.89 created 2013
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Pathway |
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Orthology |
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Genes |
» show all
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Reference |
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Authors |
Proudfoot M, Kuznetsova E, Brown G, Rao NN, Kitagawa M, Mori H, Savchenko A, Yakunin AF |
Title |
General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. |
Journal |
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Sequence |
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Reference |
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Authors |
Zimmerman MD, Proudfoot M, Yakunin A, Minor W |
Title |
Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 3.1.3.89 |
ExPASy - ENZYME nomenclature database: | 3.1.3.89 |
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