EC Number   |
Natural Substrates |
|---|
    1.3.3.4 | more |
mutations of enzyme-encoding gene PPOX are involved in variegate porphyria, an acute hepatic porphyria, which is characterized by skin lesions and acute neuropsychatric/cisceral attacks due to enzyme deficiency |
| 1.3.3.4 | more |
the enzyme might be complexed in vivo with the ferrochelatase for substrate channeling |
| 1.3.3.4 | more |
enzyme PPO1 directly interacts with proteins MORF2, MORF9, or MORF8, interaction analysis, overview. The RNA editing function of PPO1 depends on its interaction with MORFs |
| 1.3.3.4 | more |
the enzyme from Leishmania major also shows a physiological ferrochelatase activity |
| 1.3.3.4 | protoporphyrinogen IX + 3 O2 |
- |
| 1.3.3.4 | protoporphyrinogen IX + 3 O2 |
during heme and chlorophyll biosynthesis, the flavin-dependent protoporphyrinogen IX oxidase catalyzes the six-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. In the following step, iron is inserted into protoporphyrin IX by ferrochelatase. The two enzymes are organized in an enzyme complex, overview |
| 1.3.3.4 | protoporphyrinogen IX + O2 |
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III |
| 1.3.3.4 | protoporphyrinogen-IX + 3 O2 |
- |
| 1.3.3.4 | protoporphyrinogen-IX + 3 O2 |
does not utilize O2 but 2,6-dichlorophenolindophenol as electron acceptor |
| 1.3.3.4 | protoporphyrinogen-IX + 3 O2 |
penultimate step of heme and chlorophyll biosynthesis |
