Regulation of peptide bond cis/trans isomerization by enzyme catalysis and its implication in physiological processes

被引：197

作者：

Fischer, G ^{[1
]}

Aumüller, T ^{[1
]}

机构：

[1] Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle An Der Saale, Germany

来源：

REVIEWS OF PHYSIOLOGY, BIOCHEMISTRY AND PHARMACOLOGY, VOL 148 | 2004年 / 148卷

关键词：

D O I：

10.1007/s10254-003-0011-3

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：

In some cases, the slow rotational movement underlying peptide bond cis/trans isomerizations is found to control the biological activity of proteins. Peptide bond cis/trans isomerases as cyclophilins, Fk506-binding proteins, parvulins, and bacterial hsp70 generally assist in the interconversion of the polypeptide substrate cis/trans isomers, and rate acceleration is the dominating mechanism of action in cells. We present evidence disputing the hypothesis that some of the molecular properties of these proteins play an auxiliary role in enzyme function.

引用

页码：105 / 150

页数：46

共 248 条

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