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Literature summary for 1.23.5.1 extracted from

  • Fufezan, C.; Simionato, D.; Morosinotto, T.
    Identification of key residues for pH dependent activation of violaxanthin de-epoxidase from Arabidopsis thaliana (2012), PLoS ONE, 7, e35669.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.23.5.1

Activating Compound

Activating Compound Comment Organism Structure
additional information VDE activation is triggered by a pH reduction in the thylakoids lumen occurring under saturating light, mechanism of the VDE activation, overview. VDE activation relies on a robust and redundant network, in which the four residues D98, D117, H168 and D206 play a major role Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
D117A site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
D117A the mutant shows 40% of wild type activity Arabidopsis thaliana
D206I site-directed mutagenesis, the mutant shows 56% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
D206I the mutant shows 44% of wild type activity Arabidopsis thaliana
D86A site-directed mutagenesis, the mutant shows 19% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
D86A the mutant shows 86% of wild type activity Arabidopsis thaliana
D98L site-directed mutagenesis, the mutant shows 41% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
D98L the mutant shows 59% of wild type activity Arabidopsis thaliana
D98L/D117A site-directed mutagenesis, the mutant shows 59% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
D98L/D117A the mutant shows 41% of wild type activity Arabidopsis thaliana
D98L/D117A/D206I site-directed mutagenesis, the mutant shows 84% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
D98L/D117A/D206I the mutant shows 16% of wild type activity Arabidopsis thaliana
D98L/D117A/D206I/H168A the mutant shows 6% of wild type activity Arabidopsis thaliana
D98L/D117A/D206I/H168A site-directed mutagenesis, the mutant shows 94% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
H168A site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme Arabidopsis thaliana
H168A the mutant shows 20% of wild type activity Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid
-
 Arabidopsis thaliana 9579
-
thylakoid lumen Arabidopsis thaliana 9579
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
antheraxanthin + L-ascorbate Arabidopsis thaliana
-
 zeaxanthin + L-dehydroascorbate + H2O
-
 ?
violaxanthin + 2 L-ascorbate Arabidopsis thaliana
-
 zeaxanthin + 2 L-dehydroascorbate + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
antheraxanthin + L-ascorbate
-
 Arabidopsis thaliana zeaxanthin + L-dehydroascorbate + H2O
-
 ?
violaxanthin + 2 L-ascorbate
-
 Arabidopsis thaliana zeaxanthin + 2 L-dehydroascorbate + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
VDE
-
 Arabidopsis thaliana

Expression

Organism Comment Expression
Arabidopsis thaliana enzyme activation is triggered by a pH reduction in the thylakoids lumen occurring under saturating light up

General Information

General Information Comment Organism
evolution the four putative activation residues D98, D117, H168 and D206 play are all conserved in plants but not in diatoms Arabidopsis thaliana
additional information molecular dynamics and simulations, overview Arabidopsis thaliana
physiological function the carotenoid zeaxanthin, synthesized from violaxanthin by violaxanthin de-epoxidase plays a major role in the protection from excess illumination Arabidopsis thaliana