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Literature summary for 1.3.3.4 extracted from

  • Dayan, F.E.; Daga, P.R.; Duke, S.O.; Lee, R.M.; Tranel, P.J.; Doerksen, R.J.
    Biochemical and structural consequences of a glycine deletion in the alpha-8 helix of protoporphyrinogen oxidase (2010), Biochim. Biophys. Acta, 1804, 1548-1556.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
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 Amaranthus tuberculatus

Inhibitors

Inhibitors Comment Organism Structure
acifluorfen
-
Amaranthus tuberculatus
lactofen
-
Amaranthus tuberculatus
MC-15608
-
Amaranthus tuberculatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
protoporphyrinogen IX about, pH 7.4, temperature not specified in the publication Amaranthus tuberculatus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Amaranthus tuberculatus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoporphyrinogen IX + 3 O2 Amaranthus tuberculatus
-
protoporphyrin IX + 3 H2O2
-
?

Organism

Organism UniProt Comment Textmining
Amaranthus tuberculatus Q0NZW5 Gly210 deletion PPO mutant
-
Amaranthus tuberculatus Q0NZW6 PPO wild-type
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrinogen IX + 3 O2
-
Amaranthus tuberculatus protoporphyrin IX + 3 H2O2
-
?

Subunits

Subunits Comment Organism
More 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 Amaranthus tuberculatus

Synonyms

Synonyms Comment Organism
PPO
-
Amaranthus tuberculatus
R-PPO
-
Amaranthus tuberculatus
S-PPO
-
Amaranthus tuberculatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Amaranthus tuberculatus

Cofactor

Cofactor Comment Organism Structure
FAD
-
Amaranthus tuberculatus

General Information

General Information Comment Organism
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 Amaranthus tuberculatus
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 Amaranthus tuberculatus