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
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broadleaf
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target-site
- agriculture
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postemergence
- glufosinate
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waterhemp
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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 (Cofactor
Cofactor on EC 1.3.3.4 - protoporphyrinogen oxidase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
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
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FAD
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required, binding site, structure, and mechanism, roles of 59 arginine residues and glycine residues in the flavin binding site in catalysis and cofactor binding
FAD
a FAD molecule is non-covalently bound to domain I, binding structure, overview
FAD
ab initio quantum mechanics calculations are performed for FAD optimization at the HF/6-31+G level to determine the electrostatic potential by using the restrained electrostatic potential (RESP) method according to the Merz-Singh-Kollman scheme
FAD
analysis of the FAD binding region and binding structures using wild-type and mutant enzymes, detailed overview. Ser20 mutants can still bind FAD, but polarity in this position is favourable, yet not essential for the integrity of FAD binding. Glu39 mutants suggest that a negative charge at position 39 is clearly favoured for interaction with the ribose ring of FAD, as all non-conservative replacements can not bind sufficient FAD. Asp441 appears not to be directly involved in FAD binding but rather in stabilizing FAD, and polarity in this position appears important. Trp408 may play a role in orientating or stabilizing the bound substrate during catalysis, and a non-polar (or slightly polar) residue is favoured at this position. Aromaticity in this position appears not to be critical
FAD
binding structure analysis through molecular docking using the crystal structure of Nicotiana tabacum mitochondrial PPO enzyme, overview
FAD
binding structure analysis through molecular docking using the crystal structure of Nicotiana tabacum mitochondrial PPO enzyme, overview
FAD
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the FAD cofactor present in the enzyme is proposed to mediate in electron transfer from the enzyme to plastoquinone
