Glycosidase mechanisms: Anatomy of a finely tuned catalyst

被引:776
作者
Zechel, DL [1 ]
Withers, SG [1 ]
机构
[1] Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z1, Canada
关键词
D O I
10.1021/ar970172+
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
In order to accelerate the hydrolysis of glycosidic bonds by factors approaching 10(17)-fold, glycosidases have evolved finely tuned active sites optimally configured for transition-state stabilization. Structural analyses of various enzyme complexes representing stable intermediates along the reaction coordinate, in conjunction with detailed mechanistic studies on wild-type and mutant enzymes, have delineated the contributions of nucleophilic and general acid/base catalysis, as well as the roles of noncovalent interactions, to these impressive rate enhancements.
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页码:11 / 18
页数:8
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共 58 条
[1]   1-aza sugars, apparent transition state analogues of equatorial glycoside formation/cleavage [J].
Bols, M .
ACCOUNTS OF CHEMICAL RESEARCH, 1998, 31 (01) :1-8
[2]   The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase [J].
Burmeister, WP ;
Cottaz, S ;
Driguez, H ;
Iori, R ;
Palmieri, S ;
Henrissat, B .
STRUCTURE, 1997, 5 (05) :663-675
[3]   STRUCTURES AND MECHANISMS OF GLYCOSYL HYDROLASES [J].
DAVIES, G ;
HENRISSAT, B .
STRUCTURE, 1995, 3 (09) :853-859
[4]  
Davies G., 1998, COMPREHENSIVE BIOL C, P119
[5]   Snapshots along an enzymatic reaction coordinate:: Analysis of a retaining β-glycoside hydrolase [J].
Davies, GJ ;
Mackenzie, L ;
Varrot, A ;
Dauter, M ;
Brzozowski, AM ;
Schülein, M ;
Withers, SG .
BIOCHEMISTRY, 1998, 37 (34) :11707-11713
[6]  
Deslongchamps P., 1983, Stereoelectronic Effects in Organic Chemistry
[7]  
GEBLER J, 1992, J BIOL CHEM, V267, P12559
[8]  
Heightman TD, 1999, ANGEW CHEM INT EDIT, V38, P750, DOI 10.1002/(SICI)1521-3773(19990315)38:6<750::AID-ANIE750>3.0.CO
[9]  
2-6
[10]   Structural and sequence-based classification of glycoside hydrolases [J].
Henrissat, B ;
Davies, G .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1997, 7 (05) :637-644