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Literature summary extracted from

  • Nagpal, A.; Valley, M.P.; Fitzpatrick, P.F.; Orville, A.M.
    Crystallization and preliminary analysis of active nitroalkane oxidase in three crystal forms (2004), Acta Crystallogr. Sect. D, 60, 1456-1460.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.3.1 expression in Escherichia coli strains BL21(DE3) and methionine auxotroph B834(DE3) Fusarium oxysporum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.3.1 purified recombinant wild-type enzyme, crystallization of the native enzyme in 2 different crystal forms and of the selenomethionine-labeled enzyme in a third one, hanging drop vapour diffusion method, sodium cacodylate buffer, pH 7.5, containing spermidine hydrochloride, and PEG 4000 at varying concentrations for all 3 mixtures, crystal form 2 requires addition of 1,6-hexanediol at 8% w/v, crystal form 3 requires DTT at 10 mM, 4°C, 10-14 days, X-ray diffraction structure determinations and analysis at 3.2-2.0 A resolution or below, three-wavelength MAD data Fusarium oxysporum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.3.1 48162
-
 x * 48162, amino acid sequence calculation, enzyme forms homodimers and homotetramers with a preference for the latter Fusarium oxysporum

Organism

EC Number Organism UniProt Comment Textmining
1.7.3.1 Fusarium oxysporum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.3.1 recombinant enzyme from Escherichia coli Fusarium oxysporum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.3.1 nitroalkane + O2 + H2O neutral nitroalkanes Fusarium oxysporum aldehyde or ketone + nitrite + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.3.1 oligomer x * 48162, amino acid sequence calculation, enzyme forms homodimers and homotetramers with a preference for the latter Fusarium oxysporum

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.3.1 FAD oxidized FAD is bound to the active site Fusarium oxysporum