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

Author:

Kang Dong-Min1,Tanaka Kosei2,Takenaka Shinji12,Ishikawa Shu3,Yoshida Ken-ichi23

Affiliation:

1. Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Japan

2. Organization of Advanced Science and Technology, Kobe University, Kobe, Japan

3. Department of Science, Technology and Innovation, Graduate School of Science, Technology and Innovation, Kobe University, Kobe, Japan

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.

Funder

Ministry of Education, Culture, Sports, Science, and Technology

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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