Protein motions promote catalysis

被引：99

作者：

Tousignant, A ^{[1
]}

Pelletier, JN ^{[1
]}

机构：

[1] Univ Montreal, Dept Chim, Montreal, PQ H3C 3J7, Canada

来源：

CHEMISTRY & BIOLOGY | 2004年 / 11卷 / 08期

关键词：

D O I：

10.1016/j.chembiol.2004.06.007

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：

A relationship between molecular dynamics motions of noncatalytic residues and enzyme activity has recently been proposed. We present examples where mutations either near or distal from the active site residues modify internal enzyme motion with resulting modification of catalysis. A better understanding of internal protein motions correlated to catalysis will lead to a greater insight into enzyme function.

引用

页码：1037 / 1042

页数：6

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