1.3.3.4: protoporphyrinogen oxidase
This is an abbreviated version!
For detailed information about protoporphyrinogen oxidase, go to the full flat file.
Word Map on EC 1.3.3.4
-
1.3.3.4
-
herbicide
-
heme
-
porphyria
-
variegate
-
chlorophyl
-
weed
-
coproporphyrinogen
-
acifluorfen
-
ferrochelatase
-
diphenyl
-
tetrapyrrole
-
porphobilinogen
-
ppo-inhibiting
-
amaranthus
-
flumioxazin
-
tuberculatus
-
glyphosate
-
neurovisceral
-
5-aminolevulinic
-
oxyfluorfen
-
acetolactate
-
uroporphyrinogen
-
fomesafen
-
oxadiazon
-
broadleaf
-
target-site
-
agriculture
-
postemergence
-
glufosinate
-
waterhemp
-
herbicide-resistant
-
porphyrinogenic
-
coproporphyria
-
diphenylether
-
oxidase-inhibiting
-
rudis
-
glyphosate-resistant
-
sauer
-
diagnostics
-
medicine
-
drug development
-
mesotrione
-
analysis
- 1.3.3.4
-
herbicide
- heme
- porphyria
- variegate
-
chlorophyl
-
weed
- coproporphyrinogen
- acifluorfen
-
ferrochelatase
-
diphenyl
- tetrapyrrole
- porphobilinogen
-
ppo-inhibiting
- amaranthus
- flumioxazin
- tuberculatus
- glyphosate
-
neurovisceral
-
5-aminolevulinic
- oxyfluorfen
- acetolactate
- uroporphyrinogen
- fomesafen
- oxadiazon
-
broadleaf
-
target-site
- agriculture
-
postemergence
- glufosinate
-
waterhemp
-
herbicide-resistant
-
porphyrinogenic
- coproporphyria
- diphenylether
-
oxidase-inhibiting
- rudis
-
glyphosate-resistant
-
sauer
- diagnostics
- medicine
- drug development
- mesotrione
- analysis
Reaction
Synonyms
HemG, HemG-type PPO, HemG-type protoporphyrinogen IX oxidase, hemY, hPPO, H_N10, H_N40, H_N90, LMJF_06_1280, mtPPO, MxPPOX, MxProtox, PPO, PPO1, ppo1-1, PPO2, PPOX, PPOX I, PPX1, PPX2, protein YfeX, protogen oxidase, protoporphyrinogen IX oxidase, protoporphyrinogen IX oxidase 1, protoporphyrinogen oxidase, protoporphyrinogen oxidase IX, protoporphyrinogenase, protox, Protox enzyme, R-PPO, Rs-slr1790 protein, S-PPO, Salk_143057, YfeX
ECTree
Advanced search results
General Information
General Information on EC 1.3.3.4 - protoporphyrinogen oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
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
evolution
HemG proteins are highly related to flavodoxin proteins, crystal structure analysis
-
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
malfunction
-
when PPO is inhibited, protoporphyrin IX accumulates to cause light-dependent membrane damage
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
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
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
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
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
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
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
-
protoporphyrinogen IX oxidase is the last common enzyme of heme and chlorophyll biosynthesis
metabolism
-
protoporphyrinogen oxidase acts in the tetrapyrrole biosynthetic pathway that leads to the formation of both heme and chlorophylls
metabolism
-
protoporphyrinogen oxidase is the last common enzyme in the biosynthetic pathway leading to heme synthesis
metabolism
the enzyme catalyzes the penultimate step in the heme biosynthesis
metabolism
Thermosynechococcus vestitus
-
the flavin-dependent protoporphyrinogen IX oxidase catalyzes the six-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX in heme and chlorophyll biosynthesis. In the following step, iron is inserted into protoporphyrin IX by ferrochelatase. The two enzymes are organized in an enzyme complex, overview
metabolism
PPO plays an important part in the heme/chlorophyll biosynthetic pathway
metabolism
-
protoporphyrinogen IX oxidase is an essential enzyme catalyzing the last common step in the pathway leading to heme and chlorophyll biosynthesis
metabolism
protoporphyrinogen IX oxidase is an essential enzyme catalyzing the last common step in the pathway leading to heme and chlorophyll biosynthesis
metabolism
protoporphyrinogen IX oxidase is an essential enzyme catalyzing the last common step in the pathway leading to heme and chlorophyll biosynthesis
metabolism
-
protoporphyrinogen IX oxidase is an essential enzyme catalyzing the last common step in the pathway leading to heme biosynthesis
metabolism
-
the enzyme catalyzes the aromatization of protoporphyrinogen IX to protoporphyrin IX, a central step in heme biosynthesis
metabolism
enzyme PPO1 is the last enzyme in the common pathway to chlorophyll and heme biosynthesis
metabolism
protoporphyrinogen oxidase (PPO) is a key enzyme in the tetrapyrrole biosynthesis
metabolism
-
PPO plays an important part in the heme/chlorophyll biosynthetic pathway
-
metabolism
-
the enzyme catalyzes the aromatization of protoporphyrinogen IX to protoporphyrin IX, a central step in heme biosynthesis
-
-
protoporphyrinogen oxidase is one of the most important action targets of commercial herbicides
physiological function
-
protoporphyrinogen oxidase (HemG) and heme metabolism are important for Chlamydia trachomatis infectivity
physiological function
-
YfeX effectively decolorizes the dyes alizarin red and Cibacron blue F3GA and has peroxidase activity with pyrogallal but not guiacol. YfeX oxidizes protoporphyrinogen to protoporphyrin in vitro. But it shows no dechelation of heme to free porphyrin as purified enzyme or in cellular extracts of Escherichia coli overexpressing YfeX. YfeX is a typical dye-decolorizing peroxidase (or DyP) and not a dechelatase
physiological function
protoporphyrinogen IX oxidase catalyzes the oxidation of protoporphyrinogen IX (protogen IX) to protoporphyrin IX (proto IX) in the haem/chlorophyll biosynthetic pathway
physiological function
protoporphyrinogen oxidase (PPOX) i the penultimate enzyme in the heme biosynthetic pathway catalysing the six electron oxidation of protoporphyrinogen-IX to protoporphyrin-IX, in the presence of flavin adenine dinucleotide (FAD) and oxygen
physiological function
the enzyme also shows a physiological ferrochelatase activity. Partial heme biosynthesis from phagocyte-derived heme precursors in Leishmania major is highly probable. It serves most probably to haemoprotein formation during the amastigotic state in the macrophage, model for the intracellular localization of heme synthetic enzymes and heme trafficking in Leishmania major amastigotes, overview
physiological function
the role for PPO1 does not only involve tetrapyrrole biosynthesis but also distinct regulation of plastid RNA editing in higher plants. PPO1 interacts with plastid-localized MORF proteins, which in turn, additionally interact with two PPR proteins, chlororespiratory reduction 28 (CRR28) and organelle transcript processing 82 (OTP82), and a DYW domain-containing protein, DYW1. The interaction with MORFs is critical for the RNA editing function of PPO1. The catalytic activity of PPO1 requires efficient FAD and protoporphyrinogen IX binding
physiological function
-
protoporphyrinogen oxidase (HemG) and heme metabolism are important for Chlamydia trachomatis infectivity
-
Gly210 plays a key role in the alphaL helix-capping motif at the C-terminus of the alpha-8 helix which helps to stabilize the helix, protein homology modelling, three-dimensional model, and molecular dynamics simulations of the mutant enzymes, overview
additional information
Gly210 plays a key role in the alphaL helix-capping motif at the C-terminus of the alpha-8 helix which helps to stabilize the helix, protein homology modelling, three-dimensional model, and molecular dynamics simulations of the mutant enzymes, overview
additional information
-
Gly210 plays a key role in the alphaL helix-capping motif at the C-terminus of the alpha-8 helix which helps to stabilize the helix, protein homology modelling, three-dimensional model, and molecular dynamics simulations of the mutant enzymes, overview
additional information
Gly210 plays a key role in the alphaL helix-capping motif at the C-terminus of the alpha-8 helix which helps to stabilize the helix, protein homology modelling, three-dimensional model, and molecular dynamics simulations of the wild-type enzyme, overview
additional information
Gly210 plays a key role in the alphaL helix-capping motif at the C-terminus of the alpha-8 helix which helps to stabilize the helix, protein homology modelling, three-dimensional model, and molecular dynamics simulations of the wild-type enzyme, overview
additional information
-
Gly210 plays a key role in the alphaL helix-capping motif at the C-terminus of the alpha-8 helix which helps to stabilize the helix, protein homology modelling, three-dimensional model, and molecular dynamics simulations of the wild-type enzyme, overview
additional information
-
substrate binding model, molecular docking studies, overview. The protogen is surrounded by R97, L166, R168, G169, V170, F331, L334, M368, and FAD in hPPO. Ring A of protogen interacts with R168 and is kept in position by hydrophobic interaction with M368. Ring B of protogen is sandwiched between hPPO residue V170 and FAD
additional information
-
substrate binding model, molecular docking studies, overview. The protogen is surrounded by R98, F172, A174, G175, T176, F353, L356, F392, and FAD in tobacco mtPPO. Possible role of R98 during the substrate recognition mechanism,
additional information
-
Vibrio fischeri, an organism that can utilize heme as an iron source when grown under iron limitation, is able to grow with heme as the sole source of iron when its YfeX homolog is absent. Plasmid-driven expression of Escherichia coli YfeX in Vibrio fischeri grown with heme does not result in accumulation of protoporphyrin
additional information
analysis of binding mode of protogen IX in the Nicotiana tabacum protoporphyrinogen IX oxidase (mtPPO) by performing a computational docking followed by molecular simulations, quantum mechanics calculations, and an integrated analysis, overview. Several potential key residues, e.g. Thr70, Arg233, Ser235, Ser474 and Lys477, are identified. Residue Arg98 is necessary for binding of protogen IX. Comparison of the Nicotiana tabacum enzyme with the human enzyme. Modeling of ligand binding structures
additional information
-
analysis of binding mode of protogen IX in the Nicotiana tabacum protoporphyrinogen IX oxidase (mtPPO) by performing a computational docking followed by molecular simulations, quantum mechanics calculations, and an integrated analysis, overview. Several potential key residues, e.g. Thr70, Arg233, Ser235, Ser474 and Lys477, are identified. Residue Arg98 is necessary for binding of protogen IX. Comparison of the Nicotiana tabacum enzyme with the human enzyme. Modeling of ligand binding structures
additional information
the active site residues are essential for HemG catalysis, spectral analysis of heme biosynthesis, overview