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Purinergic Signal. 2012 Sep;8(3):437-502. doi: 10.1007/s11302-012-9309-4. Epub 2012 May 4.

Cellular function and molecular structure of ecto-nucleotidases.

Author information

1
Institute of Cell Biology and Neuroscience, Molecular and Cellular Neurobiology, Biologicum, Goethe-University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt am Main, Germany. h.zimmermann@bio.uni-frankurt.de

Abstract

Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ecto-nucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5'-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

PMID:
22555564
PMCID:
PMC3360096
DOI:
10.1007/s11302-012-9309-4
[Indexed for MEDLINE]
Free PMC Article

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