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Literature summary for 1.3.5.1 extracted from

  • Cecchini, G.; Thompson, C.R.; Ackrell, B.A.; Westenberg, D.J.; Dean, N.; Gunsalus, R.P.
    Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide (1986), Proc. Natl. Acad. Sci. USA, 83, 8898-8902.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
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

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Escherichia coli
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General Information

General Information Comment Organism
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