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
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1.3.3.4
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herbicide
-
heme
-
porphyria
-
variegate
-
chlorophyl
-
weed
-
coproporphyrinogen
-
acifluorfen
-
ferrochelatase
-
diphenyl
-
tetrapyrrole
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porphobilinogen
-
ppo-inhibiting
-
amaranthus
-
flumioxazin
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tuberculatus
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glyphosate
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neurovisceral
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5-aminolevulinic
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oxyfluorfen
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acetolactate
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uroporphyrinogen
-
fomesafen
-
oxadiazon
-
broadleaf
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target-site
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agriculture
-
postemergence
-
glufosinate
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waterhemp
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herbicide-resistant
-
porphyrinogenic
-
coproporphyria
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diphenylether
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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
1.3.3.4 protoporphyrinogen oxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.3.3.4 - protoporphyrinogen oxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen-I + 3 O2
coproporphyrin-I + 3 H2O2
-
oxidized at less than 11% of the rate of protoporphyrinogen-IX
-
-
?
protoporphyrinogen-IX + 3 2,6-dichlorophenolindophenol
protoporphyrin-IX + 3 reduced 2,6-dichlorophenolindophenol
Megalodesulfovibrio gigas
-
anaerobic bacterium, electron acceptor other than O2 required, does not utilize NAD(P)+, FAD or FMN
-
?
uroporphyrinogen-I + 3 O2
uroporphyrin-I + 3 H2O2
-
oxidized at less than 11% of the rate of protoporphyrinogen-IX
-
-
?
mesoporphyrinogen-IX + 3 O2
mesoporphyrin-IX + 3 H2O2
-
100times lower activity
-
-
?
mesoporphyrinogen-IX + 3 O2
mesoporphyrin-IX + 3 H2O2
-
oxidized at the same rate as protoporphyrinogen-IX
-
-
?
mesoporphyrinogen-IX + 3 O2
mesoporphyrin-IX + 3 H2O2
-
10% of the rate of protoporphyrinogen-IX
-
-
?
mesoporphyrinogen-IX + 3 O2
mesoporphyrin-IX + 3 H2O2
-
20% of the rate of protoporphyrinogen-IX
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin + 3 H2O2
Bacillus subtilis PPO shows a broad substrate specificity involving residue Y366 at a site adjacent to substrate and FAD cofactor, modeling and docking studies and structure-function relationship, overview
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin + 3 H2O2
-
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
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin + 3 H2O2
Thermosynechococcus vestitus
-
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
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step before the chlorophyl and heme synthesis diverge in plants
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate enzyme in the heme biosynthesis, several mutations of the enzyme encoding gene are responsible for variegate porphyria
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
the penultimate step in the heme biosynthesis, enzyme deficiency causes variegate porphyria
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
roles of 59 arginine residues and glycine residues in the flavin binding site in catalysis and cofactor binding
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
Megalodesulfovibrio gigas
-
similar enzyme from Desulfovibrio gigas does not use O2 as electron acceptor, but 2,6-dichlorophenol-indophenol
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
Megalodesulfovibrio gigas
-
does not utilize O2 but 2,6-dichlorophenolindophenol as electron acceptor
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
Megalodesulfovibrio gigas
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
enzyme deficiency causes variegate porphyria, bringing about e.g. light-sensitivity of human skin
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
-
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
protoporphyrinogen-IX + 3 O2
protoporphyrin-IX + 3 H2O2
-
penultimate step of heme and chlorophyll biosynthesis
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
bsPPO has a broader substrate specificity compared to other PPOs, substrate binding structure comparison of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
bsPPO has a broader substrate specificity compared to other PPOs, substrate binding structure comparison of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
bsPPO has a broader substrate specificity compared to other PPOs, substrate binding structure comparison of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
cytochrome c is found to enhance the catalytic rate of Drosophila melanogaster protoporphyrinogen oxidase under reduced oxygen conditions, and cytochrome c becomes reduced during protoporphyrinogen oxidase catalysis
-
-
?
additional information
?
-
-
holo-YfeX effectively oxidizes both protoporphyrinogen IX and coproporphyrinogen III, see for EC 1.3.3.3, to their corresponding porphyrins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
development of a binding model for the protogen substrate protoporphyrinogen IX through extensive computational simulations, analysis of essential active site residues (protogen surrounded by R97, L166, R168, G169, V170, F331, L334, M368, and FAD in hPPO) and mechanism of substrate recognition, docking uses the crystal structure of Nicotiana tabacum mitochondrial PPO enzyme and of the human PPO enzyme, overview
-
-
?
additional information
?
-
the enzyme from Leishmania major also shows a physiological ferrochelatase activity
-
-
?
additional information
?
-
purified recombinant Leishmania major HemG gene product reveals PPO activity in vitro using different ubiquinones and triphenyltetrazolium as electron acceptors. FMN is identified as the physiological Leishmania major HemG cofactor
-
-
?
additional information
?
-
the enzyme might be complexed in vivo with the ferrochelatase for substrate channeling
-
-
?
additional information
?
-
-
the enzyme might be complexed in vivo with the ferrochelatase for substrate channeling
-
-
?
additional information
?
-
development of a binding model for the protogen substrate protoporphyrinogen IX through extensive computational simulations, analysis of essential active site residues (protogen surrounded by R98, F172, A174, G175, T176, F353, L356, F392, and FAD in tobacco mtPPO) and mechanism of substrate recognition, docking uses the crystal structure of Nicotiana tabacum mitochondrial PPO enzyme and of the human PPO enzyme, overview
-
-
?
