Document Detail

myo-Inositol catabolism in Bacillus subtilis.
MedLine Citation:
PMID:  18310071     Owner:  NLM     Status:  MEDLINE    
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 CO(2) 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 CO(2).
Ken-ichi Yoshida; Masanori Yamaguchi; Tetsuro Morinaga; Masaki Kinehara; Maya Ikeuchi; Hitoshi Ashida; Yasutaro Fujita
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-02-28
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  283     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2008 Apr 
Date Detail:
Created Date:  2008-04-14     Completed Date:  2008-06-10     Revised Date:  2009-07-17    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  10415-24     Citation Subset:  IM    
Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University Kobe 657-8501, Japan.
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MeSH Terms
Aldehyde-Lyases / metabolism
Bacillus subtilis / metabolism*
Bacterial Proteins / metabolism
Carbon-Carbon Lyases / physiology
DNA / metabolism
DNA-Binding Proteins / metabolism
Dihydroxyacetone Phosphate / metabolism
Fructose-Bisphosphate Aldolase / physiology
Gene Expression Regulation, Bacterial*
Gluconates / metabolism
Glucuronic Acid / metabolism
Hydrolases / physiology
Inositol / metabolism*
Models, Biological
Models, Chemical
Phosphotransferases / physiology
Protein Binding
Repressor Proteins / metabolism
Reg. No./Substance:
0/Bacterial Proteins; 0/DNA-Binding Proteins; 0/Gluconates; 0/Repressor Proteins; 526-95-4/gluconic acid; 57-04-5/Dihydroxyacetone Phosphate; 576-37-4/Glucuronic Acid; 6917-35-7/Inositol; 9007-49-2/DNA; EC 2.7.-/Phosphotransferases; EC 3.-/Hydrolases; EC 4.1.-/Carbon-Carbon Lyases; EC 4.1.2.-/Aldehyde-Lyases; EC Aldolase

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