Oxidation-reduction and activation properties of chloroplast fructose 1,6-bisphosphatase with mutated regulatory site.

@article{Balmer2001OxidationreductionAA,
  title={Oxidation-reduction and activation properties of chloroplast fructose 1,6-bisphosphatase with mutated regulatory site.},
  author={Yves Balmer and Anne Lise Stritt-Etter and Masakazu Hirasawa and Jean Pierre Jacquot and Eliane K{\'e}ryer and David B. Knaff and Peter Sch{\"u}rmann},
  journal={Biochemistry},
  year={2001},
  volume={40 50},
  pages={15444-50}
}
The concentration of Mg(2+) required for optimal activity of chloroplast fructose 1,6-bisphosphatase (FBPase) decreases when a disulfide, located on a flexible loop containing three conserved cysteines, is reduced by the ferredoxin/thioredoxin system. Mutation of either one of two regulatory cysteines in this loop (Cys155 and Cys174 in spinach FBPase) produces an enzyme with a S(0.5) for Mg(2+) (0.6 mM) identical to that observed for the reduced WT enzyme and significantly lower than the S(0.5… CONTINUE READING