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
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heme
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porphyria
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variegate
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chlorophyl
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weed
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coproporphyrinogen
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acifluorfen
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ferrochelatase
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diphenyl
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tetrapyrrole
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porphobilinogen
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ppo-inhibiting
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amaranthus
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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
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fomesafen
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oxadiazon
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broadleaf
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target-site
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agriculture
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postemergence
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glufosinate
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waterhemp
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herbicide-resistant
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porphyrinogenic
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coproporphyria
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diphenylether
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oxidase-inhibiting
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rudis
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glyphosate-resistant
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sauer
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diagnostics
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medicine
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drug development
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mesotrione
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analysis
- 1.3.3.4
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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
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Subunits
Subunits on EC 1.3.3.4 - protoporphyrinogen oxidase
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dimer
monomer
additional information
?
x * 56000, recombinant wild-type enzyme and mutant V311M, SDS-PAGE
monomer
Bacillus subtilis PPO is unique among PPO family members in that it is a soluble monomer
monomer
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Bacillus subtilis PPO is unique among PPO family members in that it is a soluble monomer
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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
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
additional information
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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
additional information
modeling and docking studies and structure-function relationship, overview. Homology modelling and structure comparisons, overview
additional information
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modeling and docking studies and structure-function relationship, overview. Homology modelling and structure comparisons, overview
additional information
prototypical PPO enzyme structure consists of three domains: a FAD-binding domain, a substrate binding domain and a membrane-binding domain, structure analysis and comparison, overview
additional information
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prototypical PPO enzyme structure consists of three domains: a FAD-binding domain, a substrate binding domain and a membrane-binding domain, structure analysis and comparison, overview
additional information
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prototypical PPO enzyme structure consists of three domains: a FAD-binding domain, a substrate binding domain and a membrane-binding domain, structure analysis and comparison, overview
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additional information
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secondary structure analysis, wild-type and mutant enzymes, structure/function relationship mutant R59W
additional information
dimer interface structure, domain structure, overview
additional information
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dimer interface structure, domain structure, overview
additional information
Thermosynechococcus vestitus
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analysis of the enzyme in complex with ferrochelatase by mass spectrometry and immunohistochemical determination, overview