Water in enzyme reactions: biophysical aspects of hydration-dehydration processes

Authors
Citation
Y. Pocker, Water in enzyme reactions: biophysical aspects of hydration-dehydration processes, CELL MOL L, 57(7), 2000, pp. 1008-1017
Citations number
103
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
57
Issue
7
Year of publication
2000
Pages
1008 - 1017
Database
ISI
SICI code
1420-682X(200007)57:7<1008:WIERBA>2.0.ZU;2-X
Abstract
Water has been recognized as one of the major structuring factors in biolog ical macromolecules. Indeed, water clusters influence many aspects of biolo gical function, and the water-protein interaction has long been recognized as a major determinant of chain folding, conformational stability, internal dynamics, binding specificity and catalysis. I discuss here several themes arising from recent progress in understanding structural aspects of 'direc t' and 'indirect' ligands in terms of enzyme-substrate interactions, and th e role of water bridges in enzyme catalysis. The review also attempts to il luminate issues relating to efficiency, through solvent interactions associ ated with enzymic specificity, and versatility. Over the pears, carbonic an hydrase (CA; carbonate hydrolyase, EC 4.2.1.1) has played a significant rol e in the continuing delineation of principles underlying the role of water in enzyme reactions. As a result of its pronounced catalytic power and robu st constitution CA was transformed into a veritable 'laboratory' in which a ctive site mechanisms were rigorously tested and explored.