Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CuCl2 | 3 mM, 60% inhibition | Thermotoga maritima | |
HgCl2 | 3 mM, 98% inhibition | Thermotoga maritima | |
hydrocortisone | 3 mM, 5% inhibition | Thermotoga maritima | |
Quinacrine | 3 mM, 46% inhibition | Thermotoga maritima | |
Quinine | 3 mM, 23% inhibition | Thermotoga maritima |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.042 | - |
NADH | pH 7.8, 80°C | Thermotoga maritima | |
0.043 | - |
O2 | pH 7.8, 80°C | Thermotoga maritima |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
46000 | - |
1 * 54000 + 1 * 46000, SDS-PAGE | Thermotoga maritima |
54000 | - |
1 * 54000 + 1 * 46000, SDS-PAGE | Thermotoga maritima |
90000 | - |
gel filtration | Thermotoga maritima |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
NADH + H+ + O2 | Thermotoga maritima | an oxygen-removing system present in Thermotoga maritima is proposed to work in two steps: firstly by converting O2 to hydrogen peroxide by the NADH oxidase, and secondly by reducing the hydrogen peroxide to water by an NADH peroxidase or rubrerythrin or alkyl hydroperoxide reductase | NAD+ + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | - |
- |
- |
Oxidation Stability | Organism |
---|---|
apparently, the enzyme in the cell extract is more resistant to oxygen inactivation than the purified enzyme. Purified enzyme samples exposed to air exhibit a decrease in enzyme activity. The inactivation rate of NADH oxidase activity is dependent on oxygen concentration. The times required for the loss of 50% of the enzyme activity from the purified enzyme are about 20 min and 40 min for oxygen concentrations of 20% (v/v) and 1% (v/v), respectively. However, the times required for the loss of 50% of the enzyme activity from the cell extract aree about 60 min and 360 min for oxygen concentration of 20% (v/v) and 1% (v/v), respectively | Thermotoga maritima |
Purification (Comment) | Organism |
---|---|
purified under strictly anaerobic conditions | Thermotoga maritima |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
144 | - |
pH 7.0, 80°C | Thermotoga maritima |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
NADH + H+ + O2 | an oxygen-removing system present in Thermotoga maritima is proposed to work in two steps: firstly by converting O2 to hydrogen peroxide by the NADH oxidase, and secondly by reducing the hydrogen peroxide to water by an NADH peroxidase or rubrerythrin or alkyl hydroperoxide reductase | Thermotoga maritima | NAD+ + H2O2 | - |
? | |
NADH + H+ + O2 | the enzyme is highly specific for NADH, no activity with NADPH. Highest activity using O2 as an electron acceptor. Compared to lower activities for benzyl viologen (20%) and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB, 7%), while no activity is observed when FAD, FMN, or riboflavin is used as the electron acceptor | Thermotoga maritima | NAD+ + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 1 * 54000 + 1 * 46000, SDS-PAGE | Thermotoga maritima |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
- |
Thermotoga maritima |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
t1/2: 100 min | Thermotoga maritima |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
at 80°C | Thermotoga maritima |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoprotein. The enzyme contains 1.9 mol of FAD per mol native enzyme | Thermotoga maritima | |
NADH | the enzyme is highly specific for NADH, no activity with NADPH | Thermotoga maritima |