STEREOCHEMICAL, MECHANISTIC, AND STRUCTURAL FEATURES OF ENZYME-CATALYZED PHOSPHATE MONOESTER HYDROLYZES

Authors
Citation
D. Gani et J. Wilkie, STEREOCHEMICAL, MECHANISTIC, AND STRUCTURAL FEATURES OF ENZYME-CATALYZED PHOSPHATE MONOESTER HYDROLYZES, Chemical Society reviews, 24(1), 1995, pp. 55-63
Citations number
36
Categorie Soggetti
Chemistry
Journal title
ISSN journal
03060012
Volume
24
Issue
1
Year of publication
1995
Pages
55 - 63
Database
ISI
SICI code
0306-0012(1995)24:1<55:SMASFO>2.0.ZU;2-O
Abstract
Phosphoryl transfer is intimately involved at all levels of cellular c ontrol. This short review summarizes and highlights our understanding of the chemistry of phosphate monoester hydrolyses in a wide range of different enzymic systems. The article draws attention to the similari ties and differences in the diverse array of mechanisms that are emplo yed by Nature in mediating phosphate ester hydrolysis and identifies t rends that are related to the substrate specificity of phosphatases.