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Literature summary for 1.7.2.3 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

General Stability Organism
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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
41
-
purified tungsten-substituted enzyme Escherichia coli

Substrates and Products (Substrate)

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

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

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