Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition?

被引：128

作者：

Ruelland, E ^{[1
]}

Miginiac-Maslow, M ^{[1
]}

机构：

[1] Univ Paris Sud, Inst Biotechnol Plantes, CNRS, UMR 8618, F-91405 Orsay, France

来源：

TRENDS IN PLANT SCIENCE | 1999年 / 4卷 / 04期

关键词：

D O I：

10.1016/S1360-1385(99)01391-6

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Studies on redox signaling and light regulation of chloroplast enzymes have highlighted the importance of the ferredoxin-thioredoxin thiol-disulfide interchange cascade. Recent research has focused on the intramolecular mechanism by which the reduction status of a chloroplast enzyme affects its catalytic properties, and site-directed mutagenesis has been used to identify the regulatory cysteines involved. For some of the thiol-regulated enzymes, structure-function studies have revealed that the complex conformational changes that occur might be associated with disulfide isomerization and auto-inhibition. Transgenic approaches indicate that this regulation constitutes a rapid means to adjust enzyme activity to metabolic needs.

引用

页码：136 / 141

页数：6

共 38 条

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