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
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chlorophyl
-
weed
- coproporphyrinogen
- acifluorfen
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ferrochelatase
-
diphenyl
- tetrapyrrole
- porphobilinogen
-
ppo-inhibiting
- amaranthus
- flumioxazin
- tuberculatus
- glyphosate
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neurovisceral
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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
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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 (Engineering
Engineering on EC 1.3.3.4 - protoporphyrinogen oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S305L
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the amino acid exchange causes an insensitivity for the herbicide butafenacil and a KpnI site for detection of gene targeting events
Y426M
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the amino acid exchange causes an insensitivity for the herbicide butafenacil and a KpnI site for detection of gene targeting events
F227R
the mutant shows reduced activity compared to the wild-type enzyme
I176A
the mutant shows reduced activity compared to the wild-type enzyme
K71A
the mutant shows reduced activity compared to the wild-type enzyme
P64A
the mutant shows reduced activity compared to the wild-type enzyme
V311M
site-directed mutagenesis, mutant shows similar kinetics compared to the wild-type enzyme, but slightly decreased activity dependent on pH, and NaCl, Tween 20, and imidazole concentrations
Y366A
site-directed mutagenesis, the mutant enzyme shows 10% of wild-type enzyme activity
Y366E
site-directed mutagenesis, the mutant enzyme shows 1% of wild-type enzyme activity
Y366H
site-directed mutagenesis, the mutant enzyme shows 10% of wild-type enzyme activity
G58S
V389M
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resistant against inhibition with S-23142, no changes in phenotype
A172V
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site-directed mutagenesis, 99.8% reduced activity compared to the wild-type enzyme, 99% complementation of enzyme-deficient Escherichia coli strain SAS38X
D143V
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site-directed mutagenesis, 99.6% reduced activity compared to the wild-type enzyme, 89% complementation of enzyme-deficient Escherichia coli strain SAS38X
del281H
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
F331A
F331T
G11A
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site-directed mutagenesis, 0.02% activity compared to the wild-type enzyme
G14A
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site-directed mutagenesis, 42.6% activity compared to the wild-type enzyme
G169A
G232R
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
G40E
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
G453R
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site-directed mutagenesis, nearly inactive mutant, but 89% complementation of enzyme-deficient Escherichia coli strain SAS38X
G453V
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
G9A
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site-directed mutagenesis, 0.52% activity compared to the wild-type enzyme
H20P
I12T
naturally occurring mutation in a finnish variegate porphyria patient, genotype-phenotype analysis, highly reduced activity
I283N
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naturally occurring mutation involved in pathology of variegate porphyria
L154P
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site-directed mutagenesis, 99.6% reduced activity compared to the wild-type enzyme, 93% complementation of enzyme-deficient Escherichia coli strain SAS38X
L15F
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site-directed mutagenesis, 97.4% reduced activity compared to the wild-type enzyme, 49% complementation of enzyme-deficient Escherichia coli strain SAS38X
L166N
L295P
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
L334V
L401F
naturally occurring mutation in a finnish variegate porphyria patient, genotype-phenotype analysis, inactive mutant
L444P
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
L73P
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site-directed mutagenesis, 97.6% reduced activity compared to the wild-type enzyme, complete complementation of enzyme-deficient Escherichia coli strain SAS38X
L85P
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
M368K
M368Q
R152C
R168C
R168H
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site-directed mutagenesis, 99.8% reduced activity compared to the wild-type enzyme, 68% complementation of enzyme-deficient Escherichia coli strain SAS38X
R168S
R38P
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site-directed mutagenesis, 99.2% reduced activity compared to the wild-type enzyme, 59% complementation of enzyme-deficient Escherichia coli strain SAS38X
R59I
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site-directed mutagenesis, 1.5% activity compared to the wild-type enzyme
R59K
R59S
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site-directed mutagenesis, 2.6% activity compared to the wild-type enzyme
R59W
R97G
S350P
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
V158M
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site-directed mutagenesis, 91.8% reduced activity compared to the wild-type enzyme, 97% complementation of enzyme-deficient Escherichia coli strain SAS38X
V170T
V282D
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
V290L
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site-directed mutagenesis, 98.8% reduced activity compared to the wild-type enzyme, 93% complementation of enzyme-deficient Escherichia coli strain SAS38X
V335G
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site-directed mutagenesis, inactive mutant, no complementation of enzyme-deficient Escherichia coli strain SAS38X
V84G
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site-directed mutagenesis, 99.8% reduced activity compared to the wild-type enzyme, 88% complementation of enzyme-deficient Escherichia coli strain SAS38X
Y348C
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site-directed mutagenesis, 8.6% activity compared to the wild-type enzyme
R142A
site-directed mutagenesis, the mutant shows 50fold reduced activity compared to the wild-type enzyme
Y134F
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E39D
site-directed mutagenesis, the enzyme mutant shows 81% reduced activity compared to the wild-type enzyme
N441I
site-directed mutagenesis, the enzyme mutant shows 84% reduced activity compared to the wild-type enzyme
N441Q
site-directed mutagenesis, the enzyme mutant shows 73% reduced activity compared to the wild-type enzyme
S20A
site-directed mutagenesis, the enzyme mutant shows 93% reduced activity compared to the wild-type enzyme
S20T
site-directed mutagenesis, the enzyme mutant shows 90% reduced activity compared to the wild-type enzyme
W408L
site-directed mutagenesis, the enzyme mutant shows 48% reduced activity compared to the wild-type enzyme
W408Y
site-directed mutagenesis, the enzyme mutant shows 82% reduced activity compared to the wild-type enzyme
F392E
F392H
L356N
L356V
L372N
L372V
N67R
N67R/S374D
N67W/S374D
R98A
R98E
R98K
S374D
additional information
G58S
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naturally occuring mutation, suppresses the reduced infectivity caused by treatment with IS-INP0341, an iron-saturated salicylidene acylhydrazide SAH INP0341
G58S
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naturally occuring mutation, suppresses the reduced infectivity caused by treatment with IS-INP0341, an iron-saturated salicylidene acylhydrazide SAH INP0341
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F331A
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site-directed mutagenesis of ring A, the mutant shows decreased activity compared to the wild-type enzyme
F331A
site-directed mutagenesis, calculation of free binding energy shifts
F331T
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site-directed mutagenesis of ring A, the mutant shows increased activity compared to the wild-type enzyme
F331T
site-directed mutagenesis, calculation of free binding energy shifts
G169A
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site-directed mutagenesis of ring C, the mutant shows decreased activity compared to the wild-type enzyme
G169A
site-directed mutagenesis, calculation of free binding energy shifts
H20P
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site-directed mutagenesis, 0.16% activity compared to the wild-type enzyme
H20P
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abolishes mitochondrial targeting, presumably through disruption of the protoporphyrinogen oxidase alpha-helix
L166N
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site-directed mutagenesis of ring C, the mutant shows decreased activity compared to the wild-type enzyme
L166N
site-directed mutagenesis, calculation of free binding energy shifts
L334V
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site-directed mutagenesis of ring A, the mutant shows highly increased activity compared to the wild-type enzyme
L334V
site-directed mutagenesis, calculation of free binding energy shifts
M368K
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site-directed mutagenesis of ring A, the mutant shows increased activity compared to the wild-type enzyme
M368K
site-directed mutagenesis, calculation of free binding energy shifts
M368Q
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site-directed mutagenesis of ring A, the mutant shows decreased activity compared to the wild-type enzyme
M368Q
site-directed mutagenesis, calculation of free binding energy shifts
R152C
naturally occurring mutation in a finnish variegate porphyria patient, genotype-phenotype analysis, highly reduced activity
R152C
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site-directed mutagenesis, 99.4% reduced activity compared to the wild-type enzyme, 86% complementation of enzyme-deficient Escherichia coli strain SAS38X
R168C
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site-directed mutagenesis, 17.5% activity compared to the wild-type enzyme
R168S
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site-directed mutagenesis of ring A, the mutant shows decreased activity compared to the wild-type enzyme
R168S
site-directed mutagenesis, calculation of free binding energy shifts
R59K
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site-directed mutagenesis, 37.6% activity compared to the wild-type enzyme
R59W
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site-directed mutagenesis, 0.28% activity compared to the wild-type enzyme, highly reduced FAD binding
R97G
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site-directed mutagenesis of ring A, the mutant shows increased activity compared to the wild-type enzyme
R97G
site-directed mutagenesis, calculation of free binding energy shifts
V170T
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site-directed mutagenesis of ring B, the mutant shows increased activity compared to the wild-type enzyme
V170T
site-directed mutagenesis, calculation of free binding energy shifts
F392E
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inferior binding of the substrate, but increased turnover rate than wild-type
F392E
site-directed mutagenesis, calculation of free binding energy shifts
F392H
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does not reveal detectable enzyme activity indicating an important role of Phe392 in substrate ring A stacking
L356N
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an only slightly inferior binding capacity compared with the wild-type and comparable catalytic PPO2 activities
L356N
site-directed mutagenesis, calculation of free binding energy shifts
L356V
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increased Km value, once the substrate is bound, catalysis is enhanced
L356V
site-directed mutagenesis, calculation of free binding energy shifts
L372N
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an only slightly inferior binding capacity compared with the wild-type and comparable catalytic PPO2 activities
L372N
site-directed mutagenesis, calculation of free binding energy shifts
L372V
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increased Km value, once the substrate is bound, catalysis is enhanced
L372V
site-directed mutagenesis, calculation of free binding energy shifts
N67W/S374D
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shows increased activity, structural constellation mimicking the human disease variegate porphyria
R98A
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site-directed mutagenesis, the mutant has a 60fold increased catalytic activity compared to the wild-type enzyme
R98A
site-directed mutagenesis, calculation of free binding energy shifts
R98E
site-directed mutagenesis, calculation of free binding energy shifts
R98K
site-directed mutagenesis, calculation of free binding energy shifts
additional information
identification of the rare naturally occuring Gly210 deletion in PPO from herbicide-resistant Amaranthus tuberculatus. this deletion does not affect the affinity of protoporphyrinogen IX nor the FAD content, but decreases the catalytic efficiency of the enzyme. The mutant shows a significant increase in the Kis for inhibitors and a switch in their interactions from competitive to mixed-type inhibition
additional information
identification of the rare naturally occuring Gly210 deletion in PPO from herbicide-resistant Amaranthus tuberculatus. this deletion does not affect the affinity of protoporphyrinogen IX nor the FAD content, but decreases the catalytic efficiency of the enzyme. The mutant shows a significant increase in the Kis for inhibitors and a switch in their interactions from competitive to mixed-type inhibition
additional information
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identification of the rare naturally occuring Gly210 deletion in PPO from herbicide-resistant Amaranthus tuberculatus. this deletion does not affect the affinity of protoporphyrinogen IX nor the FAD content, but decreases the catalytic efficiency of the enzyme. The mutant shows a significant increase in the Kis for inhibitors and a switch in their interactions from competitive to mixed-type inhibition
additional information
construction of a series of Arabidopsis thaliana PPO1 truncations (named D1-8) mutants and interaction analysis of PPO1 mutants with MORF proteins. The N-terminal portion (amino acid residues 113-157, D6) of PPO1 is sufficient for the interaction with MORF2 and MORF9, and the deletion of amino acid residues 136-157 (DELTA22aa) completely abolishes this interaction. indicating that this 22-aa region of PPO1 is critical for the interaction with MORF proteins but not sufficient. MORF2 and MORF9 interact with PPO1 through their N-terminal fragments. Construction of PPO1 with truncations in the FAD binding domain (amino acids 63-69, DELTAFAD) or two substrate binding sites (amino acids 389-395, DELTAS1 and amino acids 403-409, DELTAS2) into ppo1-1. None of the transgenes can rescue the lethal phenotype of the ppo1-1 homozygote, although the transcript level of mutant PPO1 is similar to that of endogenous PPO1 in the wild-type, confirming that the catalytic activity of PPO1 requires efficient FAD and protoporphyrinogen IX binding and indicating that PPO2 expression does not compensate for the loss of PPO1 function
additional information
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construction of a series of Arabidopsis thaliana PPO1 truncations (named D1-8) mutants and interaction analysis of PPO1 mutants with MORF proteins. The N-terminal portion (amino acid residues 113-157, D6) of PPO1 is sufficient for the interaction with MORF2 and MORF9, and the deletion of amino acid residues 136-157 (DELTA22aa) completely abolishes this interaction. indicating that this 22-aa region of PPO1 is critical for the interaction with MORF proteins but not sufficient. MORF2 and MORF9 interact with PPO1 through their N-terminal fragments. Construction of PPO1 with truncations in the FAD binding domain (amino acids 63-69, DELTAFAD) or two substrate binding sites (amino acids 389-395, DELTAS1 and amino acids 403-409, DELTAS2) into ppo1-1. None of the transgenes can rescue the lethal phenotype of the ppo1-1 homozygote, although the transcript level of mutant PPO1 is similar to that of endogenous PPO1 in the wild-type, confirming that the catalytic activity of PPO1 requires efficient FAD and protoporphyrinogen IX binding and indicating that PPO2 expression does not compensate for the loss of PPO1 function
additional information
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design of zinc finger nucleases (ZNFs)-mediated for induction of double-strand breaks at the intended recombination site enhancing the frequency of natural protoporphyrinogen oxidase (PPO) gene targeting at an artificial target locus using Agrobacterium tumefaciens-mediated floral dip transformation. The natural protoporphyrinogen oxidase gene can be conveniently utilized for gene targeting experiments. Wild-type Arabidopsis thaliana plants and plants expressing the ZFNs are transformed via floral dip transformation with a repair T-DNA with an incomplete PPO gene, missing the 5' coding region but containing two mutations rendering the enzyme insensitive to the herbicide butafenacil as well as an extra KpnI site for molecular analysis of gene targeting events. Selection on butafenacil. Analysis of repairing events, overview. One plant line contains a PPO gene repaired only at the 5' end via homologous recombination. Most plant lines contain extra randomly integrated T-DNA copies. Two plant lines do not contain extra T-DNAs, and the repaired PPO genes in these lines are transmitted to the next generation in a Mendelian fashion. Analysis of progeny gene-targeting plants
additional information
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construction of transgenic Oryza sativa plants, enzyme is targeted to the cytoplasm or the chloroplasts, mutant plant show higher enzyme and photosynthetic activities, phenotype alterations compared to wild-type plants, e.g. narrower and more horizontal leaves or increased number of tiller buds, overview
additional information
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Bacillus subtilis Protox gene Agrobacterium-mediated transformation into rice T3 transgenic lines, Protox activity is 56% higher in the transgenic line than in wild-type rice, indicating that Bacillus subtilis Protox gene produces an enzyme that is functionally active in transgenic rice line
additional information
construction of frameshift, deletion and insertion mutants, construction of N-terminally truncated mutants, determination of subcellular localization in expressing COS-1 cells, genotype-phenotype analysis of naturally occurring mutations in a finnish variegate porphyria patients, overview
additional information
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construction of frameshift, deletion and insertion mutants, construction of N-terminally truncated mutants, determination of subcellular localization in expressing COS-1 cells, genotype-phenotype analysis of naturally occurring mutations in a finnish variegate porphyria patients, overview
additional information
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identification of 9 mutation, including nonsense and deletion mutations, in the enzyme-encoding gene PPOX in italian population, mutations are associated with variegate porphyria, VP
additional information
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identification of several mutations of the enzyme encoding gene, responsible for variegate porphyria, overview
additional information
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constructs with reduction to 12 residues (PPOX12-GFP) and then subsequent increases to 14 (PPOX14-GFP), 15 (PPOX15-GFP) and 16 (PPOX16-GFP) residue constructs, lead to an abolition of mitochondrial targeting, however, a 17-residue construct (PPOX17-GFP) does effect mitochondrial targeting
additional information
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detection of a naturally mutation designated 1082-1083insC in the Swiss population that is responsible for the variegate porphyria, an autosomal dominant genetic defectand one of the acute hepatic porphyrias, overview
additional information
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transgenic rice plant lines expressing Protox with and without the tobacco plastidal transit sequence, expression level in transgenic lines TTS3 and TTS4 are lower than that in transgenic line M4
additional information
generation of a transgenic herbicide-tolerant rice expressing a protoporphyrinogen oxidase gene, evaluation of the competitive ability of transgenic vs. non-transgenic plants in herbicide treatment during field trails, phenotypes, overview
additional information
transgenic lines, expression levels of PPOX I mRNA and protein and the cellular enzyme activities are reduced to similar extents in transgenic plants grown under low- or high-light conditions, more necrotic leaf lesions are surprisingly generated under low- than under high-light exposure
additional information
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transgenic lines, expression levels of PPOX I mRNA and protein and the cellular enzyme activities are reduced to similar extents in transgenic plants grown under low- or high-light conditions, more necrotic leaf lesions are surprisingly generated under low- than under high-light exposure
additional information
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Bacillus subtilis Protox gene Agrobacterium-mediated transformation into rice T3 transgenic lines
additional information
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T2 homozygous transgenic plants expressing the Myxococcus xanthus Protox under the control of the constitutive maize ubiquitin promoter
additional information
construction of the slr1790 gene-disruption mutants, functional genetic complementation with the Arabidopsis thaliana hemY gene, overview
additional information
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construction of the slr1790 gene-disruption mutants, functional genetic complementation with the Arabidopsis thaliana hemY gene, overview
additional information
AY916795
construction of a synthetic Myxococcus xanthus Protox gene, with a sequence optimized to more closely match the codon usage and G+C content of the Arabidopsis Protox gene, decreased G+C content to 49% similar to that of Arapbidopsis
