A THIOREDOXIN-INDEPENDENT FULLY ACTIVE NADP-MALATE DEHYDROGENASE OBTAINED BY SITE-DIRECTED MUTAGENESIS

被引：21

作者：

ISSAKIDIS, E ^{[1
]}

DECOTTIGNIES, P ^{[1
]}

MIGINIACMASLOW, M ^{[1
]}

机构：

[1] UNIV PARIS 11,CNRS,URA 1128,PHYSIOL VEGETALE MOLEC,BFLT 430,F-91405 ORSAY,FRANCE

来源：

FEBS LETTERS | 1993年 / 321卷 / 01期

关键词：

MALATE-DEHYDROGENASE; THIOREDOXIN; LIGHT ACTIVATION; DISULFIDE AND SITE-DIRECTED MUTAGENESIS;

D O I：

10.1016/0014-5793(93)80620-A

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 triple cysteine mutant of sorghum leaf NADP-malate dehydrogenase has been constructed by site-directed mutagenesis, combining the previously obtained mutation of the two N-terminal cysteines with the mutation of the most internal of the two C-terminal cysteines. The construct, over-expressed in E coli, yielded an always active, dithiol-insensitive enzyme. It can be concluded that the dithiol activation of the unmodified enzyme involves a maximum of two different disulfides per subunit, and that none of the mutated cysteines is implicated in catalysis.

引用

页码：55 / 58

页数：4

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