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Literature summary for 1.23.5.1 extracted from
- Protein redox regulation in the thylakoid lumen the importance of disulfide bonds for violaxanthin de-epoxidase (2015), FEBS Lett., 589, 919-923 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | sequence analysis and site directed mutagenesis show that 12 cysteines are conserved in most photosynthetic eukaryotes and they are also fundamental for the activity of VDE from Arabidopsis thaliana, being involved in the formation of several structural/regulatory disulfide bonds | Arabidopsis thaliana |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant overexpression of tagged wild-type and mutant enzymes in Escherichia coli strain Origami B | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C118A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C14A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C21A | site-directed mutagenesis, almost inactive mutant | Arabidopsis thaliana |
| C249A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C27A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C33A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C37A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C46A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
| C50A | site-directed mutagenesis, the mutant shows 96.5% reduced activity compared to the wild-type enzyme | Arabidopsis thaliana |
| C65A | site-directed mutagenesis, the mutant shows 95.3% reduced activity compared to the wild-type enzyme | Arabidopsis thaliana |
| C72A | site-directed mutagenesis, almost inactive mutant | Arabidopsis thaliana |
| C7A | site-directed mutagenesis, the mutant shows 14.8% reduced activity compared to the wild-type enzyme | Arabidopsis thaliana |
| C9A | site-directed mutagenesis, inactive mutant | Arabidopsis thaliana |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | - |
Arabidopsis thaliana |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| thylakoid lumen | - |
Arabidopsis thaliana | 31977 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| violaxanthin + 2 L-ascorbate | Arabidopsis thaliana | overall reaction | zeaxanthin + 2 L-dehydroascorbate + 2 H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | Q39249 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant tagged wild-type and mutant enzymes from Escherichia coli strain Origami B by affinity chromatography | Arabidopsis thaliana |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Arabidopsis thaliana | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| violaxanthin + 2 L-ascorbate | overall reaction | Arabidopsis thaliana | zeaxanthin + 2 L-dehydroascorbate + 2 H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| VDE | - |
Arabidopsis thaliana |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Arabidopsis thaliana |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.9 | - |
assay at | Arabidopsis thaliana |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| L-ascorbate | - |
Arabidopsis thaliana | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | enzyme VDE is active in its completely oxidized form presenting six disulfide bonds. Redox titration show that VDE activity is sensitive to variation in redox potential, suggesting the possibility that dithiol/disulfide exchange reactions may represent a mechanism for VDE regulation | Arabidopsis thaliana |
| physiological function | violaxanthin to zeaxanthin conversion is catalyzed by the lumenal enzyme violaxanthin de-epoxidase (VDE), using ascorbate as reducing power. Enzyme VDE is activated by a decrease of pH in the lumen, occurring when light driven proton translocation across the thylakoids membrane exceeds ATPase activity. The redox potential has a major influence on enzyme VDE activity, overview | Arabidopsis thaliana |
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Release 2023.1 (January 2023)
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