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Literature summary for 1.7.2.3 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
Search for more literature for 1.7.2.3

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

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