KEGG ENZYME: 3.1.3.89

Entry

EC 3.1.3.89                 Enzyme

Name Class

Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
BRITE hierarchy

Sysname

2′-deoxyribonucleoside 5′-monophosphate phosphohydrolase

Reaction(IUBMB) Reaction(KEGG) Substrate Product 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.

History

EC 3.1.3.89 created 2013

Pathway Orthology

K08722

5′-deoxynucleotidase

K21510

5′-deoxynucleotidase

Genes  » show all
Taxonomy Reference   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   Sequence Reference   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   Sequence Other DBs

ExplorEnz – The Enzyme Database:

3.1.3.89

ExPASy – ENZYME nomenclature database:

3.1.3.89