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Literature summary extracted from

  • Yamamoto, I.; Okubo, N.; Ishimoto, M.
    Further characterization of trimethylamine N-oxide reductase from Escherichia coli, a molybdoprotein (1986), J. Biochem., 99, 1773-1779.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.2.3 1,10-phenanthroline slight Escherichia coli
1.7.2.3 EDTA 39% inhibition at 10 mM Escherichia coli
1.7.2.3 KCN 71% inhibition at 10 mM Escherichia coli
1.7.2.3 NaN3 39% inhibition at 10 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.3 0.15
-
 oxidized methyl viologen with trimethylamine N-oxide, pH 6.9 Escherichia coli
1.7.2.3 0.33
-
 Oxidized benzyl viologen with trimethylamine N-oxide Escherichia coli
1.7.2.3 0.67
-
 Trimethylamine-N-oxide with methyl viologen, pH 6.9 Escherichia coli
1.7.2.3 0.95
-
 Trimethylamine-N-oxide with benzyl viologen, pH 5.5 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.3 Iron enzyme contains 0.96 atoms of iron Escherichia coli
1.7.2.3 Molybdenum enzyme contains 1.96 atoms of molybdenum Escherichia coli
1.7.2.3 Molybdenum contains molybdopterin Escherichia coli
1.7.2.3 Zinc enzyme contains 1.52 atoms of zinc Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.3 95000
-
 2 * 95000, SDS-PAGE Escherichia coli
1.7.2.3 200000
-
 gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 Escherichia coli
-
 TMAO reductase I, the major enzyme among inducible TMAO reductases
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.3 using heat treatment, ammonium sulfate precipitation and chromatography on Bio-Gel A-1.5m, DEAE-cellulose and reactive blue-agarose Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.2.3 1620
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 alpha-picoline N-oxide + electron donor
-
 Escherichia coli alpha-picoline + H2O + oxidized electron donor
-
 ?
1.7.2.3 chlorate + electron donor
-
 Escherichia coli ?
-
 ?
1.7.2.3 hydroxylamine N-oxide + electron donor
-
 Escherichia coli hydroxylamine + H2O + oxidized electron donor
-
 ?
1.7.2.3 trimethylamine N-oxide + electron donor benzyl viologen as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?
1.7.2.3 trimethylamine N-oxide + electron donor NADH as electron donor Escherichia coli trimethylamine + oxidized electron donor + H2O
-
 ?
1.7.2.3 trimethylamine N-oxide + oxidized benzyl viologen + H+
-
 Escherichia coli trimethylamine + reduced benzyl viologen + H2O
-
 r
1.7.2.3 trimethylamine N-oxide + oxidized methyl viologen + H+
-
 Escherichia coli trimethylamine + reduced methyl viologen + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
1.7.2.3 dimer 2 * 95000, SDS-PAGE Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.7.2.3 70
-
 30 min, enzyme activity does not change Escherichia coli
1.7.2.3 75
-
 60% loss of activity Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.2.3 5.5
-
 with benzyl viologen Escherichia coli
1.7.2.3 6.9
-
 with methyl viologen Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.3 additional information the enzyme contains more than 0.4 atoms of acid-labile sulfur per molecular weight of 200000 Escherichia coli
1.7.2.3 NADH
-
 Escherichia coli