Cloned (Comment) | Organism |
---|---|
overexpressed in Escherichia coli BL21(DE3) | Lacticaseibacillus rhamnosus |
Protein Variants | Comment | Organism |
---|---|---|
C42A | produces H2O2, 90% loss of NADH oxidase activity | Lacticaseibacillus rhamnosus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Co2+ | 1 mM, 79% inhibition | Lacticaseibacillus rhamnosus | |
FAD | optimum FAD concentration for the LrNox is 0.01 mM, with 90% and 3% of maximum activity at 0.001 mM and 0.5 mM FAD, respectively. Enzyme activity decreases sharply with an increase in FAD concentration due to inhibition by FAD. More than 90% enzyme activity is lost when FAD concentration is increased from 0.01 to 0.3 mM | Lacticaseibacillus rhamnosus | |
Hg2+ | 1 mM, 85% inhibition | Lacticaseibacillus rhamnosus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0058 | - |
NADH | pH 5.6, 65°C | Lacticaseibacillus rhamnosus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
2 * 50000, SDS-PAGE | Lacticaseibacillus rhamnosus |
100000 | - |
gel filtration | Lacticaseibacillus rhamnosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lacticaseibacillus rhamnosus | - |
- |
- |
Lacticaseibacillus rhamnosus ATCC 53103 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Lacticaseibacillus rhamnosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 NADH + H+ + O2 | - |
Lacticaseibacillus rhamnosus | NAD+ + 2 H2O | - |
? | |
2 NADH + H+ + O2 | - |
Lacticaseibacillus rhamnosus ATCC 53103 | NAD+ + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 50000, SDS-PAGE | Lacticaseibacillus rhamnosus |
Synonyms | Comment | Organism |
---|---|---|
H2O-forming NADH oxidase | - |
Lacticaseibacillus rhamnosus |
LrNox | - |
Lacticaseibacillus rhamnosus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
- |
Lacticaseibacillus rhamnosus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 70 | the enzyme is not thermal-sensitive since there is an activity change of only 28% when the temperature varies in the range of 25°C to 70°C | Lacticaseibacillus rhamnosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
half-life: 55 h | Lacticaseibacillus rhamnosus |
40 | - |
half-life: 33 h | Lacticaseibacillus rhamnosus |
50 | - |
half-life: 14 h | Lacticaseibacillus rhamnosus |
60 | - |
half-life: 6.8 h | Lacticaseibacillus rhamnosus |
70 | - |
half-life: 4.2 h | Lacticaseibacillus rhamnosus |
80 | - |
half-life: 2.1 h | Lacticaseibacillus rhamnosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.6 | - |
- |
Lacticaseibacillus rhamnosus |
7 | - |
assay at | Lacticaseibacillus rhamnosus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.6 | 6 | pH 4.6: 68% of maximal activity, pH 6.0: 54% of maximal activity | Lacticaseibacillus rhamnosus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoenzyme. Optimum FAD concentration for the LrNox is 0.01 mM, with 90% and 3% of maximum activity at 0.001 mM and 0.5 mM FAD, respectively. Enzyme activity decreases sharply with an increase in FAD concentration due to inhibition by FAD. More than 90% enzyme activity is lost when FAD concentration is increased from 0.01 to 0.3 mM | Lacticaseibacillus rhamnosus |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Lacticaseibacillus rhamnosus | isoelectric focusing | - |
5 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
37700 | - |
NADH | pH 5.6, 65°C | Lacticaseibacillus rhamnosus |