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Literature summary for 1.7.3.1 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
Search for more literature for 1.7.3.1

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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]

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

Organism

Organism UniProt Comment Textmining
Fusarium oxysporum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitroethane + O2 + H2O
-
 Fusarium oxysporum ethanal + nitrite + H2O2 + H+
-
 ?

Synonyms

Synonyms Comment Organism
nitroethane oxidase
-
 Fusarium oxysporum

Turnover Number [1/s]

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

Cofactor

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

kcat/KM [mM/s]

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