Literature summary for 1.7.3.1 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.

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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]

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

Organism

Organism	UniProt	Comment	Textmining
Fusarium oxysporum	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

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