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Literature summary extracted from

  • Valley, M.P.; Fenny, N.S.; Ali, S.R.; Fitzpatrick, P.F.
    Characterization of active site residues of nitroalkane oxidase (2010), Bioorg. Chem., 38, 115-119.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.7.3.1 C397S the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme Fusarium oxysporum
1.7.3.1 S171A the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold Fusarium oxysporum
1.7.3.1 S171T the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation Fusarium oxysporum
1.7.3.1 S171V the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation Fusarium oxysporum
1.7.3.1 Y398F the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutant enzyme is less stable than the wild type enzyme Fusarium oxysporum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.3.1 0.011
-
 O2 mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 0.028
-
 O2 mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 0.029
-
 O2 mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 0.044
-
 O2 mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 0.058
-
 O2 mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 0.082
-
 O2 wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 1.9
-
 nitroethane mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 2
-
 nitroethane mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 2
-
 nitroethane mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 2.1
-
 nitroethane mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 2.3
-
 nitroethane wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 4.8
-
 nitroethane mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C 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 nitroethane + O2 + H2O
-
 Fusarium oxysporum ethanal + nitrite + H2O2 + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.7.3.1 nitroethane oxidase
-
 Fusarium oxysporum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.3.1 5.4
-
 nitroethane mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 6.2
-
 nitroethane mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 7.2
-
 nitroethane mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 7.3
-
 nitroethane mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 10.6
-
 nitroethane mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 15
-
 nitroethane wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.3.1 FAD 0.1 mM FAD is used in assay conditions Fusarium oxysporum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.7.3.1 2.2
-
 nitroethane mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 2.6
-
 nitroethane mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 3.2
-
 nitroethane mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 3.6
-
 nitroethane mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 6.3
-
 nitroethane wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 140
-
 O2 mutant enzyme S171V, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 190
-
 O2 mutant enzyme S171A, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 290
-
 O2 mutant enzyme C397S, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 310
-
 O2 wild type enzyme, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 390
-
 O2 mutant enzyme Y398F, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum
1.7.3.1 580
-
 O2 mutant enzyme S171T, in 200 mM HEPES, 0.1 mM FAD, pH 8.0, 30 °C Fusarium oxysporum