1.13.12.16: nitronate monooxygenase
This is an abbreviated version!
For detailed information about nitronate monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.16
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1.13.12.16
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nitroalkanes
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flavin
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nitroethane
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neurospora
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crassa
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fmn
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hansenula
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mrakii
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flavosemiquinone
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1-nitropropane
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denitrification
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3-nitropropionic
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ansochromogenes
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fmn-dependent
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saturnus
- 1.13.12.16
- nitroalkanes
- flavin
- nitroethane
- neurospora
- crassa
- fmn
- hansenula
- mrakii
-
flavosemiquinone
- 1-nitropropane
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denitrification
-
3-nitropropionic
- ansochromogenes
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fmn-dependent
- saturnus
Reaction
Synonyms
2-nitropropane dioxygenase, EC 1.13.11.32, NAO, ncd2, nitroalkane oxidase, nitroalkane-oxidizing enzyme, nitronate monooxygenase, nitropropane dioxygenase, NMO, NMO-Nc, NMO-Ws, nmoA, Npd1, Npd2, Npd3, Npd4, Npd5, Npd6, oxidase, nitroalkane, oxygenase, 2-nitropropane di-, P3N monooxygenase, Pa-NMO, PA4202, protein PA4202, Rv1894c, Sa-NAO
ECTree
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Cofactor
Cofactor on EC 1.13.12.16 - nitronate monooxygenase
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cytochrome c
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cytochrome c also inhibits the reaction and half-inhibition is found in the presence of 17 microM cytochrome c. The addition of cytochrome c to the reaction mixture containing 2-nitropropane and 2-nitropropane dioxygenase causes an increase in absorbance at 550 nm indicating the reduction of cytochrome c
FAD
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contains 0.95 mol of FAD per mol of enzyme. The enzyme-bound FAD is reduced by 2-nitropropane under anaerobic conditions
FMN
dependent on, stoichiometry of 0.84 FMN per 1 monomer of enzyme, noncovalently bound
FMN
contains a mol of non-covalently bound FMN per mol of subunit, contains 0.84 FMN per monomer of enzyme
FMN
present in a 1:1 stoichiometry with the protein. The tight binding of sulfite (Kd = 0.09 mM, at pH 8 and 15°C) to the enzyme and the formation of the anionic flavosemiquinone upon anaerobic incubation with alkyl nitronates are consistent with the presence of a positively charged group in proximity of the N(1)-C(2)=O atoms of the FMN cofactor
FMN
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binding of sodium nitrite to the enzyme enzymes induces spectral changes in the FMN cofactor bound at the active site of the enzyme
FMN
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binding of sodium nitrite to the enzyme enzymes induces spectral changes in the FMN cofactor bound at the active site of the enzyme
FMN
dependent on, stoichiometry of 0.84 FMN per 1 monomer of enzyme, noncovalently bound, contains a mol of non-covalently bound FMN per mol of subunit, contains 0.84 FMN per monomer of enzyme
FMN
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dependent, enzyme contains flavin mononucleotide as a prosthetic group, 2 mol of FMN per mol of subunit
FMN
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contains a tightly, but not covalently, bound flavin that is required for enzymatic activity
FMN
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contains a tightly, but not covalently, bound flavin that is required for enzymatic activity
FMN
contains a tightly, but not covalently, bound flavin that is required for enzymatic activity