Literature summary extracted from
Roche, P.A.; Moorehead, T.J.; Hamilton, G.A.
Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase (1982), Arch. Biochem. Biophys., 216, 62-73.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.13.11.27 |
1-butanol |
5% v/v, 2.9fold activation |
Sus scrofa |
|
1.13.11.27 |
1-propanol |
10% v/v, 2.1fold activation |
Sus scrofa |
|
1.13.11.27 |
acetone |
10% v/v, 5.7fold activation |
Sus scrofa |
|
1.13.11.27 |
acetonitrile |
10% v/v, 3.6fold activation |
Sus scrofa |
|
1.13.11.27 |
Cyclohexanol |
5% v/v, 4.4fold activation |
Sus scrofa |
|
1.13.11.27 |
dioxane |
10% v/v, 2.8fold activation |
Sus scrofa |
|
1.13.11.27 |
ethanol |
10% v/v, 2fold activation |
Sus scrofa |
|
1.13.11.27 |
ether |
10% v/v, 2.6fold activation |
Sus scrofa |
|
1.13.11.27 |
methanol |
10% v/v, 1.6fold activation |
Sus scrofa |
|
1.13.11.27 |
methyl-cellosolve |
10% v/v, 2.2fold activation |
Sus scrofa |
|
1.13.11.27 |
tetrahydrofuran |
10% v/v, 6.7fold activation |
Sus scrofa |
|
General Stability
EC Number |
General Stability |
Organism |
---|
1.13.11.27 |
stable to freezing and thawing |
Sus scrofa |
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.13.11.27 |
additional information |
- |
additional information |
the Km-value is the same at 25°C and at 38°C |
Sus scrofa |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.13.11.27 |
copper |
0.4 atoms of Fe per 89000 Da enzyme. Removal of copper does not correlate with loss of activity |
Sus scrofa |
|
1.13.11.27 |
Iron |
0.9 atoms of Fe per 89000 Da enzyme. Removal of iron correlates with loss of activity |
Sus scrofa |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.13.11.27 |
44000 |
- |
2 * 44000, nonidentical subunits, SDS-PAGE |
Sus scrofa |
1.13.11.27 |
50000 |
54000 |
gel filtration |
Sus scrofa |
1.13.11.27 |
89000 |
- |
equilibrium ultracentrifugation |
Sus scrofa |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.13.11.27 |
Sus scrofa |
- |
hog |
- |
Oxidation Stability
EC Number |
Oxidation Stability |
Organism |
---|
1.13.11.27 |
routinely stored in presence of O2 |
Sus scrofa |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.13.11.27 |
- |
Sus scrofa |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
1.13.11.27 |
liver |
- |
Sus scrofa |
- |
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
1.13.11.27 |
39.6 |
- |
- |
Sus scrofa |
Storage Stability
EC Number |
Storage Stability |
Organism |
---|
1.13.11.27 |
-20°C, concentrated solution, 1 mg/ml, pH 6.0, stable for 6 months or more |
Sus scrofa |
1.13.11.27 |
-20°C, on long-term storage the enzyme forms polymers, reversal by thiols |
Sus scrofa |
1.13.11.27 |
4°C, dilute solutions, 0.1 mg/ml, 100 mM sodium acetate buffer, PH 6.0, stable for up to 2 months |
Sus scrofa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.13.11.27 |
4-hydroxyphenylpyruvate + O2 |
- |
Sus scrofa |
homogentisate + CO2 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.13.11.27 |
dimer |
2 * 44000, nonidentical subunits, SDS-PAGE |
Sus scrofa |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
1.13.11.27 |
additional information |
- |
enzymatic rate increases approximately 5fold for every 10°C increase, Km-value is the same at 25°C and at 38°C |
Sus scrofa |