Journal Article

Conversion of the Coenzyme Specificity of Isocitrate Dehydrogenase by Module Replacement

Takuro Yaoi, Kentaro Miyazaki, Tairo Oshima, Yutaka Komukai and Mitiko Go

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 119, issue 5, pages 1014-1018
Published in print May 1996 | ISSN: 0021-924X
Published online May 1996 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021316
Conversion of the Coenzyme Specificity of Isocitrate Dehydrogenase by Module Replacement

Show Summary Details

Preview

The coenzyme specificity of isocitrate dehydrogenase from an extreme thennophilic bacterium was converted from NADP-dependent to NAD-dependent by replacing a “module” involved in the coenzyme binding site. The conversion was not possible with the replacement of a few residues that interact with the coenzyme. In addition, the modulereplaced mutant dehydrogenase was as stable as the original, wild type enzyme. The results support a previous hypothesis that a module is a structural and functional unit of a protein.

Keywords: coenzyme specificity; exon-shuffling hypothesis; module; molecular recognition; protein engineering

Journal Article.  0 words. 

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.