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

被引:52
作者
Pocker, Y [1 ]
机构
[1] Univ Washington, Dept Chem, Seattle, WA 98195 USA
关键词
water; enzymes; biophysical chemistry; hydration-dehydration; carbonic anhydrase;
D O I
10.1007/PL00000741
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Water has been recognized as one of the major structuring factors in biological macromolecules. Indeed, water clusters influence many aspects of biological 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 'direct' and 'indirect' ligands in terms of enzyme-substrate interactions, and the role of water bridges in enzyme catalysis. The review also attempts to illuminate issues relating to efficiency, through solvent interactions associated with enzymic specificity, and versatility. Over the pears, carbonic anhydrase (CA; carbonate hydrolyase, EC 4.2.1.1) has played a significant role in the continuing delineation of principles underlying the role of water in enzyme reactions. As a result of its pronounced catalytic power and robust constitution CA was transformed into a veritable 'laboratory' in which active site mechanisms were rigorously tested and explored.
引用
收藏
页码:1008 / 1017
页数:10
相关论文
共 104 条
[1]   BINDING IN THE TRANSITION-STATE FOR UNFOLDING OF ADENOSINE-DEAMINASE [J].
ADLER, E ;
WOLFENDEN, R .
BIOORGANIC CHEMISTRY, 1994, 22 (02) :216-225
[2]  
Anderson DE, 1993, TOPICS MOL STRUCTURA, P258
[3]  
[Anonymous], [No title captured]
[4]   THE ROLE OF CARBONIC-ANHYDRASE IN PHOTOSYNTHESIS [J].
BADGER, MR ;
PRICE, GD .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1994, 45 :369-392
[5]   Slow dynamics of water molecules on the surface of a globular protein [J].
BellissentFunel, MC ;
Zanotti, JM ;
Chen, SH .
FARADAY DISCUSSIONS, 1996, 103 :281-294
[6]   A MULTINUCLEAR LIGAND NMR INVESTIGATION OF CYANIDE, CYANATE, AND THIOCYANATE BINDING TO ZINC AND COBALT CARBONIC-ANHYDRASE [J].
BERTINI, I ;
LUCHINAT, C ;
PIERATTELLI, R ;
VILA, AJ .
INORGANIC CHEMISTRY, 1992, 31 (19) :3975-3979
[7]   THE STRUCTURE OF COBALT(II)-SUBSTITUTED CARBONIC-ANHYDRASE AND ITS IMPLICATIONS FOR THE CATALYTIC MECHANISM OF THE ENZYME [J].
BERTINI, I ;
LUCHINAT, C .
ANNALS OF THE NEW YORK ACADEMY OF SCIENCES, 1984, 429 (JUN) :89-98
[8]   X-RAY STUDIES OF WATER IN CRYSTALS OF LYSOZYME [J].
BLAKE, CCF ;
PULFORD, WCA ;
ARTYMIUK, PJ .
JOURNAL OF MOLECULAR BIOLOGY, 1983, 167 (03) :693-723
[9]   Structural analysis of inhibitor binding to human carbonic anhydrase II [J].
Boriack-Sjodin, PA ;
Zeitlin, S ;
Chen, HH ;
Crenshaw, L ;
Gross, S ;
Dantanarayana, A ;
Delgado, P ;
May, JA ;
Dean, T ;
Christianson, DW .
PROTEIN SCIENCE, 1998, 7 (12) :2483-2489
[10]   The role of water and proton-transfer processes in hydrogen-bonded chains with large proton polarizability [J].
Brzezinski, B ;
Zundel, G .
FARADAY DISCUSSIONS, 1996, 103 :363-370