Protein Variants | Comment | Organism |
---|---|---|
H121A/H124A | considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 3.2 mM compared to 1.9 mM for wild-type enzyme | Spinacia oleracea |
H124R | considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 2.1 mM compared to 1.9 mM for wild-type enzyme | Spinacia oleracea |
H124R | considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7.Km-value for ascorbate is 1.5 mM compared to 1.9 mM for wild-type enzyme | Spinacia oleracea |
H134A | considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7 | Spinacia oleracea |
H167A/H173A | considerably lower pH dependence for binding than wild-type, cooperativity value of 1.6 compared to wild-type value of 3.7. Km-value for ascorbate is 8.3 mM compared to 1.9 mM for wild-type enzyme | Spinacia oleracea |
H167R/H173R | considerably lower pH dependence for binding than wild-type, cooperativity value around 2 compared to wild-type value of 3.7. Km-value for ascorbate is 6.3 mM compared to 1.9 mM for wild-type enzyme | Spinacia oleracea |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
thylakoid | regulation of the violaxanthin de-epoxidase involves a conformational change at low lumenal pH, followed by binding of the enzyme to the thylakoid membrane. Protonation of His at low pH induces the conformational change of the enzyme, and hence indirectly regulates binding of the enzyme to the thylakoid membrane | Triticum aestivum | 9579 | - |
thylakoid | regulation of the violaxanthin de-epoxidase involves a conformational change at low lumenal pH, followed by binding of the enzyme to the thylakoid membrane. Protonation of His at low pH induces the conformational change of the enzyme, and hence indirectly regulates binding of the enzyme to the thylakoid membrane | Spinacia oleracea | 9579 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
antheraxanthin + ascorbate | Triticum aestivum | - |
zeaxanthin + dehydroascorbate + H2O | - |
? | |
antheraxanthin + ascorbate | Spinacia oleracea | - |
zeaxanthin + dehydroascorbate + H2O | - |
? | |
violaxanthin + ascorbate | Triticum aestivum | - |
antheraxanthin + dehydroascorbate + H2O | - |
? | |
violaxanthin + ascorbate | Spinacia oleracea | - |
antheraxanthin + dehydroascorbate + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Spinacia oleracea | - |
- |
- |
Triticum aestivum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
antheraxanthin + ascorbate | - |
Triticum aestivum | zeaxanthin + dehydroascorbate + H2O | - |
? | |
antheraxanthin + ascorbate | - |
Spinacia oleracea | zeaxanthin + dehydroascorbate + H2O | - |
? | |
violaxanthin + ascorbate | - |
Triticum aestivum | antheraxanthin + dehydroascorbate + H2O | - |
? | |
violaxanthin + ascorbate | - |
Spinacia oleracea | antheraxanthin + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
VDE | - |
Triticum aestivum |
VDE | - |
Spinacia oleracea |