Regulation and activity of cytosolic 5'-nucleotidase II. A bifunctional allosteric enzyme of the Haloacid Dehalogenase superfamily involved in cellular metabolism.
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 anti-tumoural and antiviral nucleoside analogues, thus being of potential therapeutic importance. cN-II is Mg2+-dependent, 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.
Bretonnet
A S
AS
Laboratoire de RMN Biomoléculaire, Université Claude Bernard--Lyon I, UMR CNRS 5180 Sciences Analytiques, ESCPE Lyon, 69622 Villeurbanne, France.
Jordheim
L P
LP
Dumontet
C
C
Lancelin
J M
JM
D015720:5'-Nucleotidase / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D000818:Animals; D019337:Hematologic Neoplasms / Q000201:enzymology; D006867:Hydrolases / Q000145:classification; D008969:Molecular Sequence Data
D006867:Hydrolases; D015720:5'-Nucleotidase; C034507:2-haloacid dehalogenase