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Literature summary for 1.8.5.3 extracted from

  • Sambasivarao, D.; Weiner, J.
    Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation (1991), J. Bacteriol., 173, 5935-5943.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information construction of a number of strains lacking portions of the chromosomal dmsABC operon. The mutant strains fail to grow anaerobically on glycerol minimal medium with dimethyl sulfoxide as the sole terminal oxidant but exhibit normal growth with nitrate, fumarate, and trimethylamine N-oxide. In vivo complementation of the mutant with plasmids carrying various dms genes, singly or in combination, reveal that the expression of all three subunits is essential to restore anaerobic growth. Expression of the DmsAB subunits without DmsC results in accumulation of the catalytically active dimer in the cytoplasm. The dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Dimethylnaphthoquinol is oxidized only by the holoenzyme. Results suggest that the membrane-intrinsic subunit is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-intrinsic subunit DmsC is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Subunits

Subunits Comment Organism
More the DmsAB dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Results suggest that the membrane-intrinsic subunit DmsC is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer Escherichia coli