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Literature summary for 1.7.3.1 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
Search for more literature for 1.7.3.1

Inhibitors

Inhibitors Comment Organism Structure
benzoate competitive Fusarium oxysporum
phenylacetic acid competitive Fusarium oxysporum

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47955
-
 2 * 47955, MALDI-TOF mass spectrometry Fusarium oxysporum
47955
-
 4 * 47955, MALDI-TOF mass spectrometry Fusarium oxysporum
147300
-
 equilibrium sedimentation Fusarium oxysporum

Organism

Organism UniProt Comment Textmining
Fusarium oxysporum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoate + H2O + O2
-
 Fusarium oxysporum ?
-
 r
nitroethane + O2
-
 Fusarium oxysporum acetaldehyde + HNO2
-
 ?
phenylacetic acid + H2O + O2
-
 Fusarium oxysporum ?
-
 r

Subunits

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

Cofactor

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