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Literature summary for 1.7.2.3 extracted from

  • Clarke, G.J.; Ward, F.B.
    Purification and properties of trimethylamine N-oxide reductase from Shewanella sp. NCMB 400 (1988), J. Gen. Microbiol., 13, 379-386.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline slight Shewanella sp.
2,2-dipyridyl slight Shewanella sp.
5,5'-dithiobis(2-nitrobenzoate)
-
Shewanella sp.
iodoacetate partial Shewanella sp.
KCN partial Shewanella sp.
Na2MoO4
-
Shewanella sp.
Na2WO4
-
Shewanella sp.
p-chloromercuribenzoate
-
Shewanella sp.
Sodium chlorate partial Shewanella sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
Trimethylamine N-oxide
-
Shewanella sp.
2.41
-
N,N-dimethyldodecylamine N-oxide
-
Shewanella sp.
6.95
-
gamma-picoline N-oxide
-
Shewanella sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Shewanella sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum enzyme contains 1.32 mol molybdenum per mol of enzyme Shewanella sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
2 MW forms, MW: 47000, SDS-PAGE in absence of reducing agents and MW: 84000, gel filtration, SDS-PAGE under reducing conditions Shewanella sp.
84000
-
2 MW forms, MW: 47000, SDS-PAGE in absence of reducing conditions and MW: 84000, gel filtration, SDS-PAGE under reducing conditions Shewanella sp.

Organism

Organism UniProt Comment Textmining
Shewanella sp.
-
marine bacterium, 2 enzyme forms
-

Purification (Commentary)

Purification (Comment) Organism
of 2 enzyme forms, using ammonium sulfate treatment, ion exchange buffer treatment, column chromatography on DEAE-Sepharose CL6B and hydroxyapatite and gel filtration on Sephacryl S-300 Shewanella sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
211.5
-
-
Shewanella sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine N-oxide + electron donor 40% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 35% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. adenosine + H2O + oxidized electron donor
-
?
gamma-picoline N-oxide + electron donor 11% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 12% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. gamma-picoline + H2O + oxidized electron donor
-
?
hydroxylamine N-oxide + electron donor 19% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 3% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. hydroxylamine + H2O + oxidized electron donor
-
?
additional information no activity with FADH2, NADH, NADPH and the reduced forms of methylene blue and N-methylphenazonium methosulphate Shewanella sp. ?
-
?
N,N-dimethyldodecylamine N-oxide + electron donor 63% relative activity to trimethylamine N-oxide with the periplasmic enzyme and 41% relative activity to trimethylamine N-oxide with the purified enzyme Shewanella sp. N,N-dimethyldodecylamine + H2O + oxidized electron donor
-
?
trimethylamine N-oxide + electron donor methyl viologen as electron donor Shewanella sp. trimethylamine + oxidized electron donor + H2O
-
?
trimethylamine N-oxide + electron donor reduced methylene blue, reduced N-methylphenazonium methosulfate as electron donors Shewanella sp. trimethylamine + oxidized electron donor + H2O
-
?
trimethylamine N-oxide + electron donor benzyl viologen as electron donor Shewanella sp. trimethylamine + oxidized electron donor + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 84000, SDS-PAGE under reducing conditions Shewanella sp.

Cofactor

Cofactor Comment Organism Structure
FAD stimulation Shewanella sp.
FMN stimulation Shewanella sp.