Application | Comment | Organism |
---|---|---|
drug development | protoporphyrinogen oxidase is one of the most important action targets of commercial herbicides | Bacillus subtilis |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged enzyme in Escherichia coli | Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acifluorfen | competitive inhibition with respect to protoporphyrinogen IX | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics, overview | Bacillus subtilis | |
0.007 | - |
protoporphyrinogen IX | pH 7.5, 25°C | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protoporphyrinogen IX + 3 O2 | Bacillus subtilis | - |
protoporphyrin + 3 H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Bacillus subtilis |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
protoporphyrinogen IX + 3 O2 | - |
Bacillus subtilis | protoporphyrin + 3 H2O2 | - |
? | |
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 | Comment | Organism |
---|---|---|
PPO | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | protoporphyrinogen oxidase is a FAD-containing enzyme | Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
malfunction | when PPO is inhibited, protoporphyrin IX accumulates to cause light-dependent membrane damage | Bacillus subtilis |
metabolism | protoporphyrinogen oxidase acts in the tetrapyrrole biosynthetic pathway that leads to the formation of both heme and chlorophylls | Bacillus subtilis |
physiological function | protoporphyrinogen oxidase is one of the most important action targets of commercial herbicides | Bacillus subtilis |