Protein Variants | Comment | Organism |
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additional information | isolation of a mutant in the frdD gene encoding the hydrophic subunit of the fumarate reductase complex. In this mutant, fumarate reductase is not as tightly bound to the membrane. The mutation in the FrdD peptide causes an almost total loss of the ability of the enzyme to oxidize either menaquinol-6, or reduced benzyl viologen. The mutation does not impair the ability of the membrane-bound fumarate reductase complex to function with succinate as substrate | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
- |
- |
General Information | Comment | Organism |
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physiological function | the FrdD subunit has an essential role both in the interaction of the enzyme with reduced menaquinone and thus in anaerobic respiration with fumarate as electron acceptor, and in binding the enzyme to the membrane | Escherichia coli |