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Literature summary extracted from

  • Styrvold, O.B.; Strom, A.R.
    Dimethylsulfoxide and trimethylamine oxide respiration of Proteus vulgaris. Evidence for a common terminal reductase system (1984), Arch. Microbiol., 140, 74-78.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.3 0.3
-
 Trimethylamine-N-oxide
-
 Proteus vulgaris
1.7.2.3 6
-
 Dimethylsulfoxide
-
 Proteus vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.3 95000
-
 gradient gel electrophoresis, gel isoelectric focusing Proteus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 Proteus vulgaris
-
 a single enzyme responsible for both trimethylamine-N-oxide and dimethylsulfoxide reductase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 dimethylsulfoxide + electron donor
-
 Proteus vulgaris ? + oxidized electron donor + H2O
-
 ?
1.7.2.3 additional information a single enzyme responsible for both trimethylamine N-oxide and dimethylsulfoxide reductase Proteus vulgaris ?
-
 ?
1.7.2.3 trimethylamine N-oxide + electron donor methyl viologen as electron donor Proteus vulgaris trimethylamine + oxidized electron donor + H2O
-
 ?