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Literature summary for 1.1.1.77 extracted from

  • Cabiscol, E.; Badia, J.; Baldoma, L.; Hidalgo, E.; Aguilar, J.; Ros, J.
    Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation (1992), Biochim. Biophys. Acta, 1118, 155-160.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ascorbate 0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min Escherichia coli
Fe2+ under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min Escherichia coli
Fe3+ 0.025 mM FeCl3 and 0.035 mM ascorbate causes a 90% enzyme inactivation after 120 min = inactivation of metal-catalyzed oxidation; several amino-acids prevent the inactivation; under aerobic conditions 0.025 mM FeCl3 causes a 50% enzyme inactivation after 120 min Escherichia coli
H2O2 under anaerobic conditions 0.01 mM Fe2+ and 0.1 mM H2O2 had the effect of 85% enzyme inactivation after 2 min, with addition of 0.0001 mM catalase the inactivation is only 25% after 2 min and with addition of 0.01 mM superoxide dismutase instead of catalse the inactivation is again 82% after 2 min Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-propane-1,2-diol + NAD+
-
Escherichia coli (R)-lactaldehyde + NADH
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Escherichia coli