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Literature summary extracted from

  • Buc, J.; Santini, C.; Giordani, R.; Czjzek, M.; Wu, L.; Giordano, G.
    Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli (1999), Mol. Microbiol., 32, 159-168.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.7.2.3 about 50% of the activity of the molybdoenzyme is lost in the presence of 0.1 M NaCl, only about 4% of its initial activity is left in the presence of 2 M NaCl, 15% of the initial activity of the tungsten-substituted enzyme is left at 2 M NaCl Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.3 0.00754
-
4-methylmorpholine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.00765
-
Trimethylamine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.00838
-
gamma-picoline N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.00991
-
alpha-picoline N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.0108
-
Pyridine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.0252
-
tetramethylene sulfoxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.0278
-
Trimethylamine N-oxide wild-type enzyme Escherichia coli
1.7.2.3 0.0278
-
diphenylsulfoxide tungsten-restored enzyme Escherichia coli
1.7.2.3 0.0316
-
Trimethylamine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 0.0421
-
4-methylmorpholine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 0.631
-
gamma-picoline N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 0.653
-
alpha-picoline N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 0.974
-
Dimethylsulfoxide tungsten-restored enzyme Escherichia coli
1.7.2.3 2.25
-
Pyridine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 10.9
-
hydroxylamine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 11.8
-
hydroxylamine N-oxide molybdenum-restored enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.3 Molybdenum in vivo tungsten substitution of the molybdoenzyme, 0.89 atoms of tungsten per mol of purified enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.3 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 41
-
purified tungsten-substituted enzyme Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.3 4-methylmorpholine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli 4-methylmorpholine + oxidized electron donor + H2O
-
?
1.7.2.3 alpha-picoline N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli alpha-picoline + H2O + oxidized electron donor
-
?
1.7.2.3 dimethylsulfoxide + electron donor tungsten-substituted enzyme Escherichia coli ? + oxidized electron donor + H2O
-
?
1.7.2.3 diphenylsulfoxide + electron donor tungsten-substituted enzyme Escherichia coli diphenylsulfide + oxidized electron donor + H2O
-
?
1.7.2.3 gamma-picoline N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli gamma-picoline + H2O + oxidized electron donor
-
?
1.7.2.3 hydroxylamine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli hydroxylamine + H2O + oxidized electron donor
-
?
1.7.2.3 pyridine N-oxide + electron donor wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli pyridine + oxidized electron donor + H2O
-
?
1.7.2.3 tetramethylene sulfoxide + electron donor tungsten-substituted enzyme Escherichia coli tetrahydrothiophene + oxidized electron donor + H2O
-
?
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 wild-type enzyme, molybdenum-restored enzyme and tungsten-restored enzyme Escherichia coli trimethylamine + oxidized electron donor + H2O
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.2.3 60
-
for molybdoenzyme, maximal activity remains the same at 80°C Escherichia coli
1.7.2.3 80
-
for tungsten-substituted enzyme, maximal level above Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.7.2.3 80
-
molybdoenzyme, after 4 min: 50% loss of activity, after 90 min: 97% loss of activity Escherichia coli
1.7.2.3 80
-
tungsten-substituted enzyme, after 90 min: more than 50% activity remains Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.2.3 26.8
-
diphenylsulfoxide tungsten-restored enzyme Escherichia coli
1.7.2.3 40.2
-
Dimethylsulfoxide tungsten-restored enzyme Escherichia coli
1.7.2.3 42.2
-
Pyridine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 43.6
-
hydroxylamine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 44.7
-
Pyridine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 52.2
-
4-methylmorpholine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 54.7
-
alpha-picoline N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 55.7
-
gamma-picoline N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 56
-
tetramethylene sulfoxide tungsten-restored enzyme Escherichia coli
1.7.2.3 57.2
-
gamma-picoline N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 58
-
Trimethylamine N-oxide tungsten-restored enzyme Escherichia coli
1.7.2.3 70.6
-
hydroxylamine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 71.4
-
4-methylmorpholine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 84.2
-
alpha-picoline N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 114
-
Trimethylamine N-oxide molybdenum-restored enzyme Escherichia coli
1.7.2.3 258
-
Trimethylamine N-oxide wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.2.3 5
-
for tungsten-substituted enzyme, a significant decrease in activity is found at pH 5.5 Escherichia coli
1.7.2.3 5 5.5 for molybdoenzyme Escherichia coli