Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Cyberlindnera mrakii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | superoxide dismutase and catalase have no effect on the enzymatic activity | Cyberlindnera mrakii |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
SDS-PAGE | Cyberlindnera mrakii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyberlindnera mrakii | Q12723 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Cyberlindnera mrakii |
Source Tissue | Comment | Organism | Textmining |
---|
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 | Comment | Organism |
---|---|---|
2-nitropropane dioxygenase | - |
Cyberlindnera mrakii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Cyberlindnera mrakii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Cyberlindnera mrakii |
8 | - |
assay at | Cyberlindnera mrakii |
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 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 |