Disulfide bond isomerization in prokaryotes

被引：48

作者：

Gleiter, Stefan

Bardwell, James C. A. ^{[1
]}

机构：

[1] Univ Michigan, Howard Hughes Med Inst, Ann Arbor, MI 48109 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2008年 / 1783卷 / 04期

关键词：

protein folding; disulfide bond formation; isomerization;

D O I：

10.1016/j.bbamcr.2008.02.009

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：

Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase. This review discusses the current knowledge about disulfide isomerization in prokaryotes. (C) 2008 Elsevier B.V. All rights reserved.

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页码：530 / 534

页数：5

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