Reaction participants Show >> << Hide
- Name help_outline 2,3-dihydroxy-3-methylbutanoate Identifier CHEBI:11424 Charge -1 Formula C5H9O4 InChIKeyhelp_outline JTEYKUFKXGDTEU-UHFFFAOYSA-M SMILEShelp_outline CC(C)(O)C(O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-methyl-2-oxobutanoate Identifier CHEBI:11851 Charge -1 Formula C5H7O3 InChIKeyhelp_outline QHKABHOOEWYVLI-UHFFFAOYSA-M SMILEShelp_outline CC(C)C(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:20936 | RHEA:20937 | RHEA:20938 | RHEA:20939 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Studies in valine biosynthesis. V. Characteristics of the purified dihydroxyacid dehydratase from spinach leaves.
KANAMORI M., WIXOM R.L.
J Biol Chem 238:998-1005(1963) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Dihydroxy acid dehydrase: an enzyme involved in the biosynthesis of isoleucine and valine.
Myers J.W.
J. Biol. Chem. 236:1414-1418(1961) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase.
Flint D.H., Emptage M.H., Finnegan M.G., Fu W., Johnson M.K.
Dihydroxy-acid dehydratase has been purified from Escherichia coli and characterized as a homodimer with a subunit molecular weight of 66,000. The combination of UV visible absorption, EPR, magnetic circular dichroism, and resonance Raman spectroscopies indicates that the native enzyme contains a ... >> More
Dihydroxy-acid dehydratase has been purified from Escherichia coli and characterized as a homodimer with a subunit molecular weight of 66,000. The combination of UV visible absorption, EPR, magnetic circular dichroism, and resonance Raman spectroscopies indicates that the native enzyme contains a [4Fe-4S]2+,+ cluster, in contrast to spinach dihydroxy-acid dehydratase which contains a [2Fe-2S]2+,+ cluster (Flint, D. H., and Emptage, M. H. (1988) J. Biol. Chem. 263, 3558-3564). In frozen solution, the reduced [4Fe-4S]+ cluster has a S = 3/2 ground state with minor contributions from forms with S = 1/2 and possibly S = 5/2 ground states. Resonance Raman studies of the [4Fe-4S]2+ cluster in E. coli dihydroxy-acid dehydratase indicate non-cysteinyl coordination of a specific iron, which suggests that it is likely to be directly involved in catalysis as is the case with aconitase (Emptage, M. H., Kent, T. A., Kennedy, M. C., Beinert, H., and Münck, E. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 4674-4678). Dihydroxy-acid dehydratase from E. coli is inactivated by O2 in vitro and in vivo as a result of oxidative degradation of the [4Fe-4S]cluster. Compared to aconitase, the oxidized cluster of E. coli dihydroxy-acid dehydratase appears to be less stable as either a cubic or linear [3Fe-4S] cluster or a [2Fe-2S] cluster. Oxidative degradation appears to lead to a complete breakdown of the Fe-S cluster, and the resulting protein cannot be reactivated with Fe2+ and thiol reducing agents. << Less