Literature summary extracted from
Reed, D.W.; Millstein, J.; Hartzell, P.L.
H(2)O(2)-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus (2001), J. Bacteriol., 183, 7007-7016.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.6.3.3 |
CHAPS |
0.2-0.5%, increases activity about twofold |
Archaeoglobus fulgidus |
|
1.6.3.3 |
n-dodecyl beta-D-maltoside |
0.5%, increases activity about twofold |
Archaeoglobus fulgidus |
|
1.6.3.3 |
Triton X-100 |
0.1-0.5%, increases activity about twofold |
Archaeoglobus fulgidus |
|
1.6.3.3 |
Tween 20 |
1.25%, increases activity about twofold |
Archaeoglobus fulgidus |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.6.3.3 |
expression in Escherichia coli |
Archaeoglobus fulgidus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.6.3.3 |
CaCl2 |
10 mM, slightly increases activity |
Archaeoglobus fulgidus |
|
1.6.3.3 |
Cd(CH3CH2COO-)2 |
10 mM, slightly increases activity |
Archaeoglobus fulgidus |
|
1.6.3.3 |
CoCl2 |
10 mM, slightly increases activity |
Archaeoglobus fulgidus |
|
1.6.3.3 |
EGTA |
10 mM, slightly increases activity |
Archaeoglobus fulgidus |
|
1.6.3.3 |
MnCl2 |
10 mM, slightly increases activity |
Archaeoglobus fulgidus |
|
1.6.3.3 |
SDS |
0.5%, completely inhibits the reaction |
Archaeoglobus fulgidus |
|
1.6.3.3 |
sodium deoxycholate |
0.5%, slightly decreases activity |
Archaeoglobus fulgidus |
|
1.6.3.3 |
ZnCl2 |
10 mM, slightly increases activity |
Archaeoglobus fulgidus |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.6.3.3 |
0.0031 |
- |
NADH |
pH 6.6, 55°C |
Archaeoglobus fulgidus |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.6.3.3 |
CuCl2 |
10 mM, 3-4fold stimulation |
Archaeoglobus fulgidus |
|
1.6.3.3 |
K3Fe(CN)6 |
10 mM, 3-4fold stimulation |
Archaeoglobus fulgidus |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.6.3.3 |
47000 |
- |
x * 47000, SDS-PAGE |
Archaeoglobus fulgidus |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.6.3.3 |
NADH + H+ + O2 |
Archaeoglobus fulgidus |
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration |
NAD+ + H2O2 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.6.3.3 |
Archaeoglobus fulgidus |
O29852 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.6.3.3 |
- |
Archaeoglobus fulgidus |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
1.6.3.3 |
1.3 |
- |
pH 6.6, 55°C |
Archaeoglobus fulgidus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.6.3.3 |
additional information |
the enzyme shows diaphorase activity in the presence of electron acceptors such as tetrazolium and cytochrome c |
Archaeoglobus fulgidus |
? |
- |
? |
|
1.6.3.3 |
NADH + H+ + O2 |
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration |
Archaeoglobus fulgidus |
NAD+ + H2O2 |
- |
? |
|
1.6.3.3 |
NADH + H+ + O2 |
no activity with beta-NADPH |
Archaeoglobus fulgidus |
NAD+ + H2O2 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.6.3.3 |
? |
x * 47000, SDS-PAGE |
Archaeoglobus fulgidus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.6.3.3 |
AF0395 |
assay at |
Archaeoglobus fulgidus |
1.6.3.3 |
NoxA2 |
- |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.6.3.3 |
55 |
- |
assay at |
Archaeoglobus fulgidus |
1.6.3.3 |
80 |
- |
- |
Archaeoglobus fulgidus |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
1.6.3.3 |
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 [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
1.6.3.3 |
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
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.6.3.3 |
6.6 |
- |
assay at |
Archaeoglobus fulgidus |
1.6.3.3 |
7.6 |
- |
- |
Archaeoglobus fulgidus |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
1.6.3.3 |
4.4 |
8.4 |
pH 4.4: about 70% of maximal activity, pH 8.4: about 90% of maximal activity |
Archaeoglobus fulgidus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.6.3.3 |
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
EC Number |
General Information |
Comment |
Organism |
---|
1.6.3.3 |
physiological function |
the enzyme may be involved in electron transfer reactions resulting in sulfate respiration |
Archaeoglobus fulgidus |