REDESIGN OF THE COENZYME SPECIFICITY OF A DEHYDROGENASE BY PROTEIN ENGINEERING

被引：690

作者：

SCRUTTON, NS ^{[1
]}

BERRY, A ^{[1
]}

PERHAM, RN ^{[1
]}

机构：

[1] UNIV CAMBRIDGE,DEPT BIOCHEM,TENNIS COURT RD,CAMBRIDGE CB2 1QW,ENGLAND

来源：

NATURE | 1990年 / 343卷 / 6253期

关键词：

D O I：

10.1038/343038a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Directed mutagenesis and molecular modelling have been used to identify a set of amino-acid side chains in glutathione reductase that confer specificity for the coenzyme NADP+. Systematic replacement of these amino acids, all of which occur in a 'fingerprint' structural motif in the NADP+-binding domain, leaves the substrate specificity unchanged but converts the enzyme into one displaying a marked preference for the coenzyme NAD+. © 1990 Nature Publishing Group.

引用

页码：38 / 43

页数：6

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