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Literature summary extracted from

  • Gadda, G.; Fitzpatrick, P.F.
    Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum (1998), Biochemistry, 37, 6154-6164.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.3.1 benzoate competitive Fusarium oxysporum
1.7.3.1 phenylacetic acid competitive Fusarium oxysporum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.3.1 2.9
-
 nitroethane
-
 Fusarium oxysporum
1.7.3.1 5.1
-
 benzoate
-
 Fusarium oxysporum
1.7.3.1 13.1
-
 phenylacetic acid
-
 Fusarium oxysporum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.3.1 47955
-
 2 * 47955, MALDI-TOF mass spectrometry Fusarium oxysporum
1.7.3.1 47955
-
 4 * 47955, MALDI-TOF mass spectrometry Fusarium oxysporum
1.7.3.1 147300
-
 equilibrium sedimentation 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 benzoate + H2O + O2
-
 Fusarium oxysporum ?
-
 r
1.7.3.1 nitroethane + O2
-
 Fusarium oxysporum acetaldehyde + HNO2
-
 ?
1.7.3.1 phenylacetic acid + H2O + O2
-
 Fusarium oxysporum ?
-
 r

Subunits

EC Number Subunits Comment Organism
1.7.3.1 dimer 2 * 47955, MALDI-TOF mass spectrometry Fusarium oxysporum
1.7.3.1 tetramer 4 * 47955, MALDI-TOF mass spectrometry Fusarium oxysporum

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.3.1 FAD 1 mol of FAD per mol of subunit is required for catalysis, reversible removal of FAD yields inactive enzyme Fusarium oxysporum