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Literature summary for 1.7.2.3 extracted from

  • Violet, M.; Medani, C.L.; Giordano, G.
    Trimethylamine N-oxide (TMAO) reductases from Escherichia coli K-12 (1985), FEMS Microbiol. Lett., 27, 85-91.
No PubMed abstract available
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Inhibitors

Inhibitors Comment Organism Structure
KCN 10-15% inhibition of the inducible and of the constitutive enzyme at 10 mM Escherichia coli
N-ethylmaleimide both inducible and constitutive enzyme are affected equally at 5 mM Escherichia coli
NaN3 5% inhibition of inducible enzyme and 50-60% inhibition of constitutive enzyme at 10 mM Escherichia coli
p-chloromercuribenzoate 2% inhibition of inducible enzyme and 50-60% inhibition of constitutive enzyme at 5 mM Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane constitutive enzyme Escherichia coli 16020
-
soluble inducible enzyme Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 a constitutive enzyme and an inducible enzyme with different properties
-

Oxidation Stability

Oxidation Stability Organism
aeration for 10 min causes 10% inactivation Escherichia coli

Storage Stability

Storage Stability Organism
-80°C, inducible and constitutive enzyme, 10% loss of activity after 15 days Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 20 min, 10% loss of activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 for inducible and constitutive enzyme Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Escherichia coli