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Literature summary for 1.7.3.1 extracted from
- Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase (2005), Arch. Biochem. Biophys., 433, 157-165.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme induction by growth on nitroethane | Fusarium oxysporum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| valerate | competitive | Fusarium oxysporum |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | thermodynamics, kinetic mechanism with nitroethane and 1-nitrobutane, isotopic effects, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane | Fusarium oxysporum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Fusarium oxysporum | the physiological role of the enzyme is the oxidation of nitroaliphatic species | ? | - |
? | |
| nitroethane + O2 + H2O | Fusarium oxysporum | - |
ethanal + nitrite + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Fusarium oxysporum | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ethylnitronate + O2 + FMNH2 = acetaldehyde + nitrite + FMN + H2O | detailed mechanism, with carbanion reaction intermediate formation, an aspartate residue is the active site base, substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane, the active site of the enzyme is a hydrophobic channel, tunneling, overview | Fusarium oxysporum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-nitroalkane + O2 + H2O | - |
Fusarium oxysporum | aldehyde + H2O2 + nitrite | - |
? | |
| 1-nitrobutane + O2 + H2O | 400fold more effective than nitroethane | Fusarium oxysporum | butyraldehyde + nitrite + H2O2 | - |
? | |
| 1-nitrohexane + O2 + H2O | - |
Fusarium oxysporum | hexanaldehyde + nitrite + H2O2 | - |
? | |
| 2-nitropropane + O2 | - |
Fusarium oxysporum | acetone + nitrite | - |
? | |
| additional information | the physiological role of the enzyme is the oxidation of nitroaliphatic species | Fusarium oxysporum | ? | - |
? | |
| additional information | enzyme does not require anionic nitroalkanes for activity, enzyme catalyzes the oxidation of a number of primary and secondary nitroalkanes to the respective aldehydes or ketones with preference for primary nitroalkanes, monotonic increase with each additional methylene group from nitroethane to 1-nitrobutane increasing kcat/Km value by 20fold, no further increase with 1-nitropentane and 1-nitrohexane | Fusarium oxysporum | ? | - |
? | |
| nitroethane + O2 + H2O | - |
Fusarium oxysporum | ethanal + nitrite + H2O2 | - |
? | |
| nitroethane + O2 + H2O | substrate CH-bond cleavage is rate limiting for the reduction of the enzyme by nitroethane | Fusarium oxysporum | ethanal + nitrite + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme structure analysis, overview | Fusarium oxysporum |
| oligomer | enzyme forms homodimers and homotetramers with a preference for the latter | Fusarium oxysporum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | enzyme belongs to the acyl-CoA dehydrogenase family of enzymes | Fusarium oxysporum |
| NAO | - |
Fusarium oxysporum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
temperature-dependency analysis | Fusarium oxysporum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
pH-profile | Fusarium oxysporum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | absolutely required, binding structure, involving Ser171, and reactive structure analysis, the apoenzyme is inactive, removal of cofactor in its active form is reversible | Fusarium oxysporum | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Ki pH profile for competitive inhibitor valerate | Fusarium oxysporum |
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Release 2023.1 (January 2023)
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