Literature summary extracted from
Tan, Y.; Sun, L.; Xi, Z.; Yang, G.F.; Jiang, D.Q.; Yan, X.P.; Yang, X.; Li, H.Y.
A capillary electrophoresis assay for recombinant Bacillus subtilis protoporphyrinogen oxidase (2008), Anal. Biochem., 383, 200-204.
Application
EC Number |
Application |
Comment |
Organism |
---|
1.3.3.4 |
drug development |
protoporphyrinogen oxidase is one of the most important action targets of commercial herbicides |
Bacillus subtilis |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.3.3.4 |
expression of His-tagged enzyme in Escherichia coli |
Bacillus subtilis |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.3.3.4 |
acifluorfen |
competitive inhibition with respect to protoporphyrinogen IX |
Bacillus subtilis |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.3.3.4 |
additional information |
- |
additional information |
steady-state kinetics, overview |
Bacillus subtilis |
|
1.3.3.4 |
0.007 |
- |
protoporphyrinogen IX |
pH 7.5, 25°C |
Bacillus subtilis |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.3.3.4 |
protoporphyrinogen IX + 3 O2 |
Bacillus subtilis |
- |
protoporphyrin + 3 H2O2 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.3.3.4 |
Bacillus subtilis |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.3.3.4 |
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography |
Bacillus subtilis |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.3.3.4 |
protoporphyrinogen IX + 3 O2 |
- |
Bacillus subtilis |
protoporphyrin + 3 H2O2 |
- |
? |
|
1.3.3.4 |
protoporphyrinogen IX + 3 O2 |
PPO catalyzes the oxygen-dependent six-electron oxidation of protoporphyrinogen IX, i.e. protogen IX, to the fully conjugated macrocycle of protoporphyrin IX, i.e. proto IX |
Bacillus subtilis |
protoporphyrin + 3 H2O2 |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.3.3.4 |
PPO |
- |
Bacillus subtilis |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.3.3.4 |
25 |
- |
assay at |
Bacillus subtilis |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.3.3.4 |
7.5 |
- |
assay at |
Bacillus subtilis |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.3.3.4 |
FAD |
protoporphyrinogen oxidase is a FAD-containing enzyme |
Bacillus subtilis |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.3.3.4 |
malfunction |
when PPO is inhibited, protoporphyrin IX accumulates to cause light-dependent membrane damage |
Bacillus subtilis |
1.3.3.4 |
metabolism |
protoporphyrinogen oxidase acts in the tetrapyrrole biosynthetic pathway that leads to the formation of both heme and chlorophylls |
Bacillus subtilis |
1.3.3.4 |
physiological function |
protoporphyrinogen oxidase is one of the most important action targets of commercial herbicides |
Bacillus subtilis |