| myo-Inositol catabolism in Bacillus subtilis. | |
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MedLine Citation:
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PMID: 18310071 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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). |
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Authors:
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Ken-ichi Yoshida; Masanori Yamaguchi; Tetsuro Morinaga; Masaki Kinehara; Maya Ikeuchi; Hitoshi Ashida; Yasutaro Fujita |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-02-28 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 283 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2008 Apr |
Date Detail:
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Created Date: 2008-04-14 Completed Date: 2008-06-10 Revised Date: 2009-07-17 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 10415-24 Citation Subset: IM |
Affiliation:
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Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University Kobe 657-8501, Japan. kenyoshi@kobe-u.ac.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aldehyde-Lyases
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metabolism Bacillus subtilis / metabolism* Bacterial Proteins / metabolism Carbon-Carbon Lyases / physiology Catalysis DNA / metabolism DNA-Binding Proteins / metabolism Dihydroxyacetone Phosphate / metabolism Fructose-Bisphosphate Aldolase / physiology Gene Expression Regulation, Bacterial* Gluconates / metabolism Glucuronic Acid / metabolism Hydrolases / physiology Hydrolysis Inositol / metabolism* Models, Biological Models, Chemical Phosphotransferases / physiology Protein Binding Repressor Proteins / metabolism |
| Chemical | |
Reg. No./Substance:
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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 4.1.2.13/Fructose-Bisphosphate Aldolase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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