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Literature summary for 1.6.3.3 extracted from
- Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus (2003), Eur. J. Biochem., 270, 2885-2994.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | 2 mM, stimulates up to 2fold | Archaeoglobus fulgidus |  |
| dithiothreitol | 2 mM, stimulates up to 2fold | Archaeoglobus fulgidus | |
| FAD | flavoprotein, addition of 0.06 mM results in 3.7fold stimulation | Archaeoglobus fulgidus | |
| FAD | flavoprotein, Addition of 0.06 mM results in about 2.5fold stimulation | Archaeoglobus fulgidus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Archaeoglobus fulgidus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | 2 mM, rapid decrease in activity to less than 10% of the activity | Archaeoglobus fulgidus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.011 | - |
NADH | pH 7.0, 70°C | Archaeoglobus fulgidus | |
| 0.06 | - |
O2 | pH 7.0, 80°C | Archaeoglobus fulgidus | |
| 0.13 | - |
NADH | pH 7.0, 80°C | Archaeoglobus fulgidus | |
| 2.9 | - |
O2 | pH 7.0, 70°C | Archaeoglobus fulgidus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | divalent cations are not required for activity | Archaeoglobus fulgidus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 48000 | - |
2 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE | Archaeoglobus fulgidus |
| 48000 | - |
4 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE | Archaeoglobus fulgidus |
| 68000 | - |
1 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE | Archaeoglobus fulgidus |
| 68000 | - |
2 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE | Archaeoglobus fulgidus |
| 70000 | - |
dimeric enzyme form, gel filtration | Archaeoglobus fulgidus |
| 94000 | - |
dimeric enzyme form, gel filtration | Archaeoglobus fulgidus |
| 152000 | - |
tetrameric enzyme form, gel filtration | Archaeoglobus fulgidus |
| 178000 | - |
tetrameric enzyme form, gel filtration | Archaeoglobus fulgidus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | O29794 | - |
- |
| Archaeoglobus fulgidus | O29985 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Archaeoglobus fulgidus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 4.05 | - |
pH 8.0, 80°C | Archaeoglobus fulgidus |
| 5.81 | - |
pH 8.0, 80°C | Archaeoglobus fulgidus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NADH + H+ + O2 | the enzyme predominantly produces H2O2. No activity with NADPH. The enzyme also shows activity with 2,6-dichloroindophenol, ferricyanide, menadione, and 2,3-dimethyl-1,4-naphthoquinone | Archaeoglobus fulgidus | NAD+ + H2O2 | - |
? | |
| NADH + H+ + O2 | the enzyme predominantly produces H2O2. No activity with NADPH. The enzyme also shows activity with 2,6-dichloroindophenol, ferricyanide, menadione, and 2,3-dimethyl-1,4-naphthoquinone. Very low activity with cytochrome c | Archaeoglobus fulgidus | NAD+ + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE | Archaeoglobus fulgidus |
| dimer | 2 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE | Archaeoglobus fulgidus |
| monomer | 1 * 68000, the enzyme exists as a monomer and to some extent as a dimer, SDS-PAGE | Archaeoglobus fulgidus |
| tetramer | 4 * 48000, the enzyme exists as a dimer and to some extent as a tetramer, SDS-PAGE | Archaeoglobus fulgidus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NoxA-1 | - |
Archaeoglobus fulgidus |
| NoxB-1 | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | 90 | 60°C: about 50% of maximal activity, 90°C: about 95% of maximal activity | Archaeoglobus fulgidus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
half-life: 40 min | Archaeoglobus fulgidus |
| 80 | - |
half-life: 40 h | Archaeoglobus fulgidus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
- |
Archaeoglobus fulgidus |
| 7 | - |
assay at | Archaeoglobus fulgidus |
| 8 | - |
- |
Archaeoglobus fulgidus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | pH 5.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity | Archaeoglobus fulgidus |
| 6.5 | 9 | pH 6.5: about 55% of maximal activity, pH 9.0: about 55% of maximal activity | Archaeoglobus fulgidus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | no activity with NADPH | Archaeoglobus fulgidus | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Archaeoglobus fulgidus | expressed constitutively under strictly anaerobic conditions. The fact that the expression of the Nox enzymes is not regulated suggests that they have some fundamental metabolic role, and not an occasional role during oxygen stress | additional information |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the fact that the expression of the Nox enzymes is not regulated suggests that they have some fundamental metabolic role, and not an occasional role during oxygen stress | Archaeoglobus fulgidus |
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