EC Number   |
General Information |
Reference |
|---|
    1.3.3.4 | evolution |
because of their importance in catalyzing protoporphyrinogen IX oxidation, the FAD, membrane, and substrate binding domains of PPO1 and PPO2 are largely conserved in species from plants to animals |
746296 |
| 1.3.3.4 | evolution |
HemG proteins are highly related to flavodoxin proteins, crystal structure analysis |
744529 |
| 1.3.3.4 | malfunction |
antioxidants restore protoporphyrinogen oxidase in variegate porphyria patients showing accumulation of heme precursors and a low rate of heme biosynthesis. Lymphocytes from variegate porphyria patients show reduced PPOX expression and present a greater susceptibility to producing H2O2 and impaired H2O2 detoxifying mechanisms. Supplementation with vitamins E and C restores PPOX expression in variegate porphyria patients and enhances glutathione reductase (GRd) and superoxide dismutase (SOD) activities. Phenotype, overview |
744837 |
| 1.3.3.4 | malfunction |
deficient activity of PPO causes the accumulation and nonenzymatic oxidation of protogen IX leading to cellular damage. For green plants, inhibition of PPO leads to the rapid bleaching and desiccation of photosynthetically active parts of the plant |
745787 |
| 1.3.3.4 | malfunction |
disruption of protoporphyrinogen IX oxidase 1 (PPO1) causes RNA editing defects in 18 of 34 known plastid RNA target sites, especially those encoded by NADH dehydrogenase-like complex (ndh) genes. Except for the ndhB-746 site, the editing efficiencies of all sites in ndhB, ndhD, ndhF, and ndhG transcripts are reduced to different extents in ppo1 compared with the wild-type, disruption of PPO1 leads to a complete loss of editing of the ndhD-2 site, where ACG is partly edited into the translation start codon AUG in the wild-type. Disruption of PPO1 severely impairs seedling growth, chlorophyll synthesis, and NDH complex accumulation. Loss of FAD or substrate binding of PPO1 does not affect RNA editing. Isozyme PPO2 expression does not compensate for the loss of PPO1 function |
746296 |
| 1.3.3.4 | malfunction |
inhibition or functional loss of PPO results in the accumulation of protogen, which can be spontaneously oxidized to proto by oxygen. As a photosensitizer, in the presence of light, proto can further induce the production of singlet oxygen, causing lipid peroxidation and cell death |
726346 |
| 1.3.3.4 | malfunction |
mutation G58S in hemG suppresses the reduced infectivity caused by treatment with IS-INP0341, an iron-saturated salicylidene acylhydrazide SAH INP0341, which specifically affects Chlamydia trachomatis infectivity with reduced generation of infectious elementary body progeny |
-, 725290 |
| 1.3.3.4 | malfunction |
partial PPO deficiency in humans causes an inherited disease known as variegated porphyria characterized by cutaneous photosensitivity and the propensity to develop acute neurovisceral crisis |
696759 |
| 1.3.3.4 | malfunction |
when PPO is inhibited, protoporphyrin IX accumulates to cause light-dependent membrane damage |
695546 |
| 1.3.3.4 | metabolism |
enzyme PPO1 is the last enzyme in the common pathway to chlorophyll and heme biosynthesis |
746296 |
