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J. Biol. Chem., Vol. 283, Issue 16, 10415-10424, April 18, 2008

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myo-Inositol Catabolism in Bacillus subtilis^*

Ken-ichi Yoshida¹, Masanori Yamaguchi, Tetsuro Morinaga, Masaki Kinehara, Maya Ikeuchi, Hitoshi Ashida, and Yasutaro Fujita^¶

From the Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University Kobe 657-8501, Central Research Laboratories, Hokko Chemical Industry Co., Ltd, Atsugi 243-0023 and ^¶Department of Biotechnology, Faculty of Life Science and Biotechnology, Fukuyama University, Fukuyama 729-0292, Japan

The iolABCDEFGHIJ operon of Bacillus subtilis is responsible for myo-inositol catabolism involving multiple and stepwise reactions. Previous studies demonstrated that IolG and IolE are the enzymes for the first and second reactions, namely dehydrogenation of myo-inositol to give 2-keto-myo-inositol and the subsequent dehydration to 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione. In the present studies the third reaction was shown to be the hydrolysis of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione catalyzed by IolD to yield 5-deoxy-D-glucuronic acid. The fourth reaction was the isomerization of 5-deoxy-D-glucuronic acid by IolB to produce 2-deoxy-5-keto-D-gluconic acid. Next, in the fifth reaction 2-deoxy-5-keto-D-gluconic acid was phosphorylated by IolC kinase to yield 2-deoxy-5-keto-D-gluconic acid 6-phosphate. IolR is known as the repressor controlling transcription of the iol operon. In this reaction 2-deoxy-5-keto-D-gluconic acid 6-phosphate appeared to be the intermediate acting as inducer by antagonizing DNA binding of IolR. Finally, IolJ turned out to be the specific aldolase for the sixth reaction, the cleavage of 2-deoxy-5-keto-D-gluconic acid 6-phosphate into dihydroxyacetone phosphate and malonic semialdehyde. The former is a known glycolytic intermediate, and the latter was previously shown to be converted to acetyl-CoA and CO₂ by a reaction catalyzed by IolA. The net result of the inositol catabolic pathway in B. subtilis is, thus, the conversion of myo-inositol to an equimolar mixture of dihydroxyacetone phosphate, acetyl-CoA, and CO₂.

Received for publication, September 26, 2007 , and in revised form, February 19, 2008.

^* This work was supported in part by a grant-in-aid for the Encouragement of Young Scientists from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (to K. Y.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Agrobioscience, Graduate School of Agricultural Science, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan. Tel.: 81-78-803-5862; Fax: 81-78-803-5815; E-mail: kenyoshi{at}kobe-u.ac.jp.

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