Enzymes
| UniProtKB help_outline | 5 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline 6-phospho-5-dehydro-2-deoxy-D-gluconate Identifier CHEBI:57949 Charge -3 Formula C6H8O9P InChIKeyhelp_outline OLUPOJQIFXQXIT-CVYQJGLWSA-K SMILEShelp_outline O[C@H](CC([O-])=O)[C@H](O)C(=O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-oxopropanoate Identifier CHEBI:33190 Charge -1 Formula C3H3O3 InChIKeyhelp_outline OAKURXIZZOAYBC-UHFFFAOYSA-M SMILEShelp_outline [H]C(=O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 20 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dihydroxyacetone phosphate Identifier CHEBI:57642 (Beilstein: 4428349) help_outline Charge -2 Formula C3H5O6P InChIKeyhelp_outline GNGACRATGGDKBX-UHFFFAOYSA-L SMILEShelp_outline C(CO)(COP([O-])(=O)[O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:13177 | RHEA:13178 | RHEA:13179 | RHEA:13180 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The pathway of myo-inositol degradation in Aerobacter aerogenes. Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic intermediates.
Anderson W.A., Magasanik B.
J Biol Chem 246:5662-5675(1971) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Myo-inositol catabolism in Bacillus subtilis.
Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H., Fujita Y.
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-inosito ... >> More
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). << Less
J. Biol. Chem. 283:10415-10424(2008) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.