Activating Compound | Comment | Organism | Structure |
---|---|---|---|
2,2'-dipyridyl | - |
Cyberlindnera mrakii | |
2,4,6-tripyridyl-s-triazine | - |
Cyberlindnera mrakii | |
o-phenanthroline | - |
Cyberlindnera mrakii |
General Stability | Organism |
---|---|
denaturation by sodium dithionite | Cyberlindnera mrakii |
gradual and irreversible loss of activity after treatment with 1% sodium lauryl sulfate or 6 M guanidine HCl, activity is reduced to 50% of its initial activity after 50 min at 37°C, complete loss of activity after 10 h | Cyberlindnera mrakii |
immediate denaturation with 8 M urea or thiourea | Cyberlindnera mrakii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | - |
Cyberlindnera mrakii | |
8-hydroxyquinoline | strong inhibition | Cyberlindnera mrakii | |
cysteine | marked decrease in enzyme activity | Cyberlindnera mrakii | |
GSH | marked decrease in enzyme activity | Cyberlindnera mrakii | |
HgCl2 | moderate and potent inhibitor | Cyberlindnera mrakii | |
additional information | EDTA does not inhibit the enzyme significantly. Iodoacetate is almost ineffective | Cyberlindnera mrakii | |
N-ethylmaleimide | - |
Cyberlindnera mrakii | |
NaHSO3 | - |
Cyberlindnera mrakii | |
NEM | - |
Cyberlindnera mrakii | |
Nitromethane | inhibits noncompetitively | Cyberlindnera mrakii | |
p-chloromercuribenzoate | - |
Cyberlindnera mrakii | |
PCMB | - |
Cyberlindnera mrakii | |
Tiron | i.e. pyrocatechol-3,5-disulfonate disodium salt; i.e. pyrocatechol-3,5-disulfonate disodium salt, strong inhibition | Cyberlindnera mrakii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
O2 | - |
Cyberlindnera mrakii | |
4.2 | - |
3-Nitro-2-butanol | neutral form of substrate | Cyberlindnera mrakii | |
6.8 | - |
nitroethane | - |
Cyberlindnera mrakii | |
6.8 | - |
3-Nitro-2-pentanol | - |
Cyberlindnera mrakii | |
21.3 | - |
2-Nitropropane | - |
Cyberlindnera mrakii | |
24.3 | - |
nitroethane | - |
Cyberlindnera mrakii | |
25.6 | - |
1-Nitropropane | - |
Cyberlindnera mrakii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe3+ | contains 1 g atom of non-heme iron per mol of enzyme | Cyberlindnera mrakii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
25000 | - |
1 * 25000 + 1 * 39000, SDS-PAGE | Cyberlindnera mrakii |
39000 | - |
1 * 25000 + 1 * 39000, SDS-PAGE | Cyberlindnera mrakii |
60000 | - |
gel filtration | Cyberlindnera mrakii |
64000 | - |
equilibrium sedimentation | Cyberlindnera mrakii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cyberlindnera mrakii | - |
- |
- |
Cyberlindnera mrakii | - |
IF0 0895 | - |
Cyberlindnera mrakii IF0 0895 | - |
IF0 0895 | - |
Purification (Comment) | Organism |
---|---|
to homogeneity | Cyberlindnera mrakii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-nitropropane + O2 | 23.4% of the activity with 2-nitropropane | Cyberlindnera mrakii | propionaldehyde + HNO2 | - |
? | |
1-nitropropane + O2 | 23.4% of the activity with 2-nitropropane | Cyberlindnera mrakii IF0 0895 | propionaldehyde + HNO2 | - |
? | |
2-nitropropane + O2 | - |
Cyberlindnera mrakii | acetone + HNO2 | - |
? | |
2-nitropropane + O2 | - |
Cyberlindnera mrakii IF0 0895 | acetone + HNO2 | - |
? | |
3-nitro-2-butanol + O2 | 13% of the activity with 2-nitropropane | Cyberlindnera mrakii | 3-hydroxy-butane-2-one + HNO2 | - |
? | |
3-nitro-2-butanol + O2 | slight oxidation | Cyberlindnera mrakii | 3-hydroxy-butane-2-one + HNO2 | - |
? | |
3-nitro-2-pentanol + O2 | 40.6% of the activity with 2-nitropropane | Cyberlindnera mrakii | 2-hydroxy-pentane-3-one + HNO2 | - |
? | |
3-nitropropionic acid + O2 | 11.7% of the activity with 2-nitropropane | Cyberlindnera mrakii | ? | - |
? | |
additional information | sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions | Cyberlindnera mrakii | ? | - |
? | |
additional information | sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions | Cyberlindnera mrakii IF0 0895 | ? | - |
? | |
nitroethane + O2 | 88% of the activity with nitroethane | Cyberlindnera mrakii | acetaldehyde + HNO2 | - |
? | |
nitroethane + O2 | 88% of the activity with nitroethane | Cyberlindnera mrakii IF0 0895 | acetaldehyde + HNO2 | - |
? | |
nitromethane + O2 | no activity | Cyberlindnera mrakii | formaldehyde + HNO2 | - |
? | |
nitromethane + O2 | is not a substrate, under anaerobic conditions. The aerobic dialysis of the enzyme treated with nitromethane causes reoxidation of only the Fe2+ | Cyberlindnera mrakii | formaldehyde + HNO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 1 * 25000 + 1 * 39000, SDS-PAGE | Cyberlindnera mrakii |
Synonyms | Comment | Organism |
---|---|---|
2-nitropropane dioxygenase | - |
Cyberlindnera mrakii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Cyberlindnera mrakii |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 45 | - |
Cyberlindnera mrakii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
when the enzyme is dialyzed against 10 mM potassium phosphate buffer (pH 7.0) immediately after reduction by dithionite, the absorption spectrum similar to that of the native enzyme appears with concomitant restoration of approximately 80% of the activity | Cyberlindnera mrakii |
8 | - |
- |
Cyberlindnera mrakii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 8.5 | - |
Cyberlindnera mrakii |
7 | 8.5 | when the enzyme is acidified to pH 3.0 and treated in the same way, the prosthetic groups do not dissociate from the protein and almost full activity remained | Cyberlindnera mrakii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | contains 0.95 mol of FAD per mol of enzyme | Cyberlindnera mrakii | |
FAD | contains 0.95 mol of FAD per mol of enzyme. The enzyme-bound FAD is reduced by 2-nitropropane under anaerobic conditions | Cyberlindnera mrakii |