Activating Compound | Comment | Organism | Structure |
---|---|---|---|
CHAPS | 0.2-0.5%, increases activity about twofold | Archaeoglobus fulgidus | |
n-dodecyl beta-D-maltoside | 0.5%, increases activity about twofold | Archaeoglobus fulgidus | |
Triton X-100 | 0.1-0.5%, increases activity about twofold | Archaeoglobus fulgidus | |
Tween 20 | 1.25%, increases activity about twofold | Archaeoglobus fulgidus |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Archaeoglobus fulgidus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CaCl2 | 10 mM, slightly increases activity | Archaeoglobus fulgidus | |
Cd(CH3CH2COO-)2 | 10 mM, slightly increases activity | Archaeoglobus fulgidus | |
CoCl2 | 10 mM, slightly increases activity | Archaeoglobus fulgidus | |
EGTA | 10 mM, slightly increases activity | Archaeoglobus fulgidus | |
MnCl2 | 10 mM, slightly increases activity | Archaeoglobus fulgidus | |
SDS | 0.5%, completely inhibits the reaction | Archaeoglobus fulgidus | |
sodium deoxycholate | 0.5%, slightly decreases activity | Archaeoglobus fulgidus | |
ZnCl2 | 10 mM, slightly increases activity | Archaeoglobus fulgidus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0031 | - |
NADH | pH 6.6, 55°C | Archaeoglobus fulgidus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
CuCl2 | 10 mM, 3-4fold stimulation | Archaeoglobus fulgidus | |
K3Fe(CN)6 | 10 mM, 3-4fold stimulation | Archaeoglobus fulgidus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
47000 | - |
x * 47000, SDS-PAGE | Archaeoglobus fulgidus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
NADH + H+ + O2 | Archaeoglobus fulgidus | the enzyme may be involved in electron transfer reactions resulting in sulfate respiration | NAD+ + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | O29852 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Archaeoglobus fulgidus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.3 | - |
pH 6.6, 55°C | Archaeoglobus fulgidus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c | Archaeoglobus fulgidus | ? | - |
? | |
NADH + H+ + O2 | the enzyme may be involved in electron transfer reactions resulting in sulfate respiration | Archaeoglobus fulgidus | NAD+ + H2O2 | - |
? | |
NADH + H+ + O2 | no activity with beta-NADPH | Archaeoglobus fulgidus | NAD+ + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 47000, SDS-PAGE | Archaeoglobus fulgidus |
Synonyms | Comment | Organism |
---|---|---|
AF0395 | assay at | Archaeoglobus fulgidus |
NoxA2 | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
assay at | Archaeoglobus fulgidus |
80 | - |
- |
Archaeoglobus fulgidus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | 90 | active from room temperature to 90°C. At 50°C, the activity of the recombinant enzyme is half that at 80°C | Archaeoglobus fulgidus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
83 | - |
pH 7.6, 40 min, the half-life of the recombinant enzyme is 12 min, the partially purified native enzyme has a half-life of 35 h | Archaeoglobus fulgidus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.6 | - |
assay at | Archaeoglobus fulgidus |
7.6 | - |
- |
Archaeoglobus fulgidus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.4 | 8.4 | pH 4.4: about 70% of maximal activity, pH 8.4: about 90% of maximal activity | Archaeoglobus fulgidus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | required for activity. 1.1 mol of FAD per mol of enzyme. The FAD cofactor is associated noncovalently with the protein | Archaeoglobus fulgidus |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme may be involved in electron transfer reactions resulting in sulfate respiration | Archaeoglobus fulgidus |