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Literature summary for 1.23.5.1 extracted from
- Overexpression of violaxanthin de-epoxidase: properties of C-terminal deletions on activity and pH-dependent lipid binding (2002), Planta, 214, 476-483.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| a full-length violaxanthin de-epoxidase and deletion mutants of the N- and C-terminal regions are expressed in Escherichia coli and Nicotiana tabacum L. cv. Xanthi. High expression of the enzyme in Escherichia coli is achieved after adding the argU gene that encodes the Escherichia coli arginine AGA tRNA. The specific activity of the violaxanthin de-epoxidase expressed in Escherichia coli is low, possibly due to incorrect folding. The transformed tobacco exhibits a 13fold to 19fold increase in VDE specific activity, indicating correct protein folding | Arabidopsis thaliana |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| DELTA1-4 | removal of 4 amino acids from the N-terminal region abolishes all violaxanthin de-epoxidase activity | Arabidopsis thaliana |
| DELTA258-349 | 71 C-terminal amino acid can be removed without affecting activity | Arabidopsis thaliana |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| thylakoid | lumen | Arabidopsis thaliana | 9579 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| VDE | - |
Arabidopsis thaliana |
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Release 2023.1 (January 2023)
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