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Literature summary extracted from

  • Gadda, G.; Fitzpatrick, P.F.
    Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole (2000), Biochemistry, 39, 1400-1405.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.7.3.1 imidazole unprotonated imidazole causes a 5fold increase in maximal velocity Fusarium oxysporum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.3.1 acetaldehyde noncompetitive inhibitor versus nitroethane due to formation of a dead-end complex between the oxidized enzyme and the product, competitive inhibitor versus oxygen Fusarium oxysporum
1.7.3.1 Butyraldehyde noncompetitive inhibitor versus nitroethane due to formation of a dead-end complex between the oxidized enzyme and the product Fusarium oxysporum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.3.1 0.023
-
 O2
-
 Fusarium oxysporum
1.7.3.1 3.3
-
 nitroethane
-
 Fusarium oxysporum

Organism

EC Number Organism UniProt Comment Textmining
1.7.3.1 Fusarium oxysporum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.3.1 1-nitrobutane + O2
-
 Fusarium oxysporum butyraldehyde + HNO2
-
 ?
1.7.3.1 1-nitrohexane + O2
-
 Fusarium oxysporum hexanaldehyde + HNO2
-
 ?
1.7.3.1 1-nitropentane + O2
-
 Fusarium oxysporum pentanaldehyde + HNO2
-
 ?
1.7.3.1 1-nitropropane + O2
-
 Fusarium oxysporum propionaldehyde + HNO2
-
 ?
1.7.3.1 2-nitropropane + O2
-
 Fusarium oxysporum acetone + HNO2
-
 ?
1.7.3.1 nitroethane + O2 at pH 7, bi-ter ping-pong mechanism with oxygen reacting with the free reduced enzyme after release of the aldehyde product Fusarium oxysporum acetaldehyde + HNO2
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.7.3.1 additional information
-
 additional information
-
 Fusarium oxysporum