Enzymes
| UniProtKB help_outline | 3 proteins |
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- Name help_outline 8-methylmenaquinone-6 Identifier CHEBI:134356 Charge 0 Formula C42H58O2 InChIKeyhelp_outline HAMLBJAJFRKXHQ-RCIYGOBDSA-N SMILEShelp_outline C1(=C(C(C=2C(=CC=CC2C1=O)C)=O)C)C/C=C(/CC/C=C(/CC/C=C(/CC/C=C(/CC/C=C(/CCC=C(C)C)\C)\C)\C)\C)\C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline succinate Identifier CHEBI:30031 (CAS: 56-14-4) help_outline Charge -2 Formula C4H4O4 InChIKeyhelp_outline KDYFGRWQOYBRFD-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 332 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 8-methylmenaquinol-6 Identifier CHEBI:134357 Charge 0 Formula C42H60O2 InChIKeyhelp_outline OCLDWCUJKRHBTH-RCIYGOBDSA-N SMILEShelp_outline C=1(C(=C(C=2C(=CC=CC2C1O)C)O)C)C/C=C(/CC/C=C(/CC/C=C(/CC/C=C(/CC/C=C(/CCC=C(C)C)\C)\C)\C)\C)\C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline fumarate Identifier CHEBI:29806 (CAS: 142-42-7) help_outline Charge -2 Formula C4H2O4 InChIKeyhelp_outline VZCYOOQTPOCHFL-OWOJBTEDSA-L SMILEShelp_outline [O-]C(=O)\C=C\C([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:51848 | RHEA:51849 | RHEA:51850 | RHEA:51851 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Production, characterization and determination of the real catalytic properties of the putative 'succinate dehydrogenase' from Wolinella succinogenes.
Juhnke H.D., Hiltscher H., Nasiri H.R., Schwalbe H., Lancaster C.R.
Both the genomes of the epsilonproteobacteria Wolinella succinogenes and Campylobacter jejuni contain operons (sdhABE) that encode for so far uncharacterized enzyme complexes annotated as 'non-classical' succinate:quinone reductases (SQRs). However, the role of such an enzyme ostensibly involved i ... >> More
Both the genomes of the epsilonproteobacteria Wolinella succinogenes and Campylobacter jejuni contain operons (sdhABE) that encode for so far uncharacterized enzyme complexes annotated as 'non-classical' succinate:quinone reductases (SQRs). However, the role of such an enzyme ostensibly involved in aerobic respiration in an anaerobic organism such as W. succinogenes has hitherto been unknown. We have established the first genetic system for the manipulation and production of a member of the non-classical succinate:quinone oxidoreductase family. Biochemical characterization of the W. succinogenes enzyme reveals that the putative SQR is in fact a novel methylmenaquinol:fumarate reductase (MFR) with no detectable succinate oxidation activity, clearly indicative of its involvement in anaerobic metabolism. We demonstrate that the hydrophilic subunits of the MFR complex are, in contrast to all other previously characterized members of the superfamily, exported into the periplasm via the twin-arginine translocation (tat)-pathway. Furthermore we show that a single amino acid exchange (Ala86-->His) in the flavoprotein of that enzyme complex is the only additional requirement for the covalent binding of the otherwise non-covalently bound FAD. Our results provide an explanation for the previously published puzzling observation that the C. jejuni sdhABE operon is upregulated in an oxygen-limited environment as compared with microaerophilic laboratory conditions. << Less