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Literature summary for 1.7.2.3 extracted from

  • Kaufmann, P.; Duffus, B.R.; Mitrova, B.; Iobbi-Nivol, C.; Teutloff, C.; Nimtz, M.; Jaensch, L.; Wollenberger, U.; Leimkuehler, S.
    Modulating the molybdenum coordination sphere of Escherichia coli trimethylamine N-oxide reductase (2018), Biochemistry, 57, 1130-1143 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S191C the mutant shows about 38% of wild type activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information not influenced by iodoacetamide Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ Escherichia coli
-
trimethylamine + 2 (ferricytochrome c)-subunit + H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
-
Escherichia coli trimethylamine + 2 (ferricytochrome c)-subunit + H2O
-
?
trimethylamine N-oxide + benzyl viologen + H+
-
Escherichia coli trimethylamine + oxidized benzyl viologen + H2O
-
?

Subunits

Subunits Comment Organism
monomer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
TMAO reductase
-
Escherichia coli
TorA
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
molybdopterin
-
Escherichia coli