Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | in the absence of photosynthetic electron flow, the chloroplast enzyme exists in its disulfide-containing form which is inactive under physiological conditions. Upon interaction with reduced thioredoxin generated in the light, the active dithiol-containing enzyme is formed | Pisum sativum |
General Stability | Organism |
---|---|
no effect of guanidine/HCl up to 0.25 M on the quarternary structure of the enzyme in its oxidized and reduced form. In the oxidized state the enzyme undergoes guanidine-dependent dissociation to the monomer with a midpoint of transition at 0.5 M. The kinetic of unfolding is significantly faster for the reduced than for the oxidized enzyme | Pisum sativum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Pisum sativum | 9507 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pisum sativum | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
renaturation of the guanidine-HCl denatured enzyme is more rapid with the reduced enzyme and occurs with higher yields, 100%, than with the oxidized enzyme, 60-80% | Pisum sativum |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Pisum sativum | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
oxaloacetate + NADPH | - |
Pisum sativum | (S)-malate + NADP+ | - |
? |