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

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• 作者：G. Fischer ^A1 and T. Aumü ; ller ^A1
• 刊名：Reviews of Physiology, Biochemistry and Pharmacology
• 出版年：2003
• 出版时间：September 2003
• 年：2003
• 卷：148
• 期：1
• 页码：105-150
• 全文大小：625 KB

文摘

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.