Bacillus subtilis iolU encodes an additional NADP+-dependent scyllo-inositol dehydrogenase. Issue 5 (4th May 2017)

• Record Type: Journal Article
• Authors: Kang, Dong-Min; Tanaka, Kosei; Takenaka, Shinji; Ishikawa, Shu; Yoshida, Ken-ichi
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 81:Issue 5(2017)
• Page Start: 1026
• Page End: 1032
• Publication Date: 2017-05-04
• Subjects: Bacillus subtilis -- inositol dehydrogenase -- myo-inositol -- NADP+/NADPH -- scyllo-inositol; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2016.1268043
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: 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 . Abstract: : Among the Gfo/Idh/MocA family paralogs in B. subtilis, IolU turned out to be an additional scyllo -inositol dehydrogenase.