Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Thioredoxin f | activates wild-type enzyme and mutant C179S | Spinacia oleracea |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Spinacia oleracea |
Protein Variants | Comment | Organism |
---|---|---|
C155S | lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S | Spinacia oleracea |
C174S | lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S | Spinacia oleracea |
C179S | mutant significantly decreases the Mg2+ requirement of the oxidized enzyme, mutant is more easily activated by thioredoxin f in comparison to wild-type enzyme | Spinacia oleracea |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Spinacia oleracea | 9507 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the oxidized wild-type enzyme is active only at very high Mg2+ concentrations, the Mg2+ requirement of oxidized and reduced forms of wild-type and mutant enzymes is compared. The reduction of the regulatory disulfide has a positive allosteric effect on the binding of the catalytically essential Mg2+ in the active site. | Spinacia oleracea |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Spinacia oleracea | - |
- |
- |