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Regulation and activity of cytosolic 5′‐nucleotidase II
Author(s) -
Bretonnet A.S.,
Jordheim L.P.,
Dumontet C.,
Lancelin J.M.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.014
Subject(s) - purine , allosteric regulation , dehalogenase , cytosol , nucleoside , biochemistry , 5' nucleotidase , enzyme , chemistry , nucleoside triphosphate , effector , nucleotidase , phosphatase , superfamily , nucleotide , biology , stereochemistry , receptor , gene
In many vertebrate tissues, cytosolic 5′‐nucleotidase II (cN‐II) either hydrolyses or phosphorylates a number of purine (monophosphorylated) nucleosides through a scheme common to the Haloacid Dehalogenase superfamily members. It possesses a pivotal role in purine cellular metabolism and it acts on antitumoural and antiviral nucleoside analogues, thus being of potential therapeutic importance. cN‐II is Mg 2+ ‐dependant, regulated and stabilised by several factors such as allosteric effectors ATP and 2,3‐DPG, although these are not directly involved in the reaction stoichiometry. We review herein the experimental knowledge currently available about this remarkable enzymatic activity.