Bacillus subtilis iolU encodes an additional NADP+-dependent scyllo-inositol dehydrogenase | Zendy

DongMin Kang | Zendy; Kosei Tanaka | Zendy; Shinji Takenaka | Zendy; Shu Ishikawa | Zendy; Kenichi Yoshida | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Bacillus subtilis iolU encodes an additional NADP+-dependent scyllo-inositol dehydrogenase

Author(s) -

DongMin Kang,

Kosei Tanaka,

Shinji Takenaka,

Shu Ishikawa,

Kenichi Yoshida

Publication year - 2017

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1080/09168451.2016.1268043

Subject(s) - bacillus subtilis , dehydrogenase , inositol , bioconversion , gene , biochemistry , biology , enzyme , function (biology) , microbiology and biotechnology , chemistry , genetics , bacteria , receptor , fermentation

Bacillus subtilis genes iolG, iolW, iolX, ntdC, yfiI, yrbE, yteT, and yulF belong to the Gfo/Idh/MocA family. The functions of iolG, iolW, iolX, and ntdC are known; however, the functions of the others are unknown. We previously reported the B. subtilis cell factory simultaneously overexpressing iolG and iolW to achieve bioconversion of myo-inositol (MI) into scyllo-inositol (SI). YulF shares a significant similarity with IolW, the NADP+-dependent SI dehydrogenase. Transcriptional abundance of yulF did not correlate to that of iol genes involved in inositol metabolism. However, when yulF was overexpressed instead of iolW in the B. subtilis cell factory, SI was produced from MI, suggesting a similar function to iolW. In addition, we demonstrated that recombinant His6-tagged YulF converted scyllo-inosose into SI in an NADPH-dependent manner. We have thus identified yulF encoding an additional NADP+-dependent SI dehydrogenase, which we propose to rename iolU.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research