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Literature summary for 1.13.12.16 extracted from

  • Mijatovic, S.; Gadda, G.
    Oxidation of alkyl nitronates catalyzed by 2-nitropropane dioxygenase from Hansenula mrakii (2008), Arch. Biochem. Biophys., 473, 61-68.
    View publication on PubMed
Search for more literature for 1.13.12.16

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Cyberlindnera mrakii

Inhibitors

Inhibitors Comment Organism Structure
additional information superoxide dismutase and catalase have no effect on the enzymatic activity Cyberlindnera mrakii

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme contains negligible amounts of iron, manganese, zinc, and copper ions, which are not catalytically relevant Cyberlindnera mrakii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 SDS-PAGE Cyberlindnera mrakii

Organism

Organism UniProt Comment Textmining
Cyberlindnera mrakii Q12723
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Cyberlindnera mrakii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + butanal
-
 ?
ethylnitronate + O2
-
 Cyberlindnera mrakii NO2- + acetaldehyde
-
 ?
hexyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + hexanal
-
 ?
additional information anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicated that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes Cyberlindnera mrakii ?
-
 ?
additional information anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicates that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes Cyberlindnera mrakii ?
-
 ?
pentyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + pentanal
-
 ?
propyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + propionaldehyde
-
 ?
propyl-2-nitronate + O2
-
 Cyberlindnera mrakii NO2- + acetone
-
 ?

Synonyms

Synonyms Comment Organism
2-nitropropane dioxygenase
-
 Cyberlindnera mrakii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Cyberlindnera mrakii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Cyberlindnera mrakii
8
-
 assay at Cyberlindnera mrakii

Cofactor

Cofactor Comment Organism Structure
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 Cyberlindnera mrakii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.6
-
 propyl-2-nitronate
-
 Cyberlindnera mrakii
112
-
 butyl-1-nitronate
-
 Cyberlindnera mrakii
121
-
 pentyl-1-nitronate
-
 Cyberlindnera mrakii
129
-
 ethylnitronate
-
 Cyberlindnera mrakii
130
-
 hexyl-1-nitronate
-
 Cyberlindnera mrakii
170
-
 propyl-1-nitronate
-
 Cyberlindnera mrakii