The corresponding mutants are active when expressed in E. coli, while C179S is inactive and can be reductively
activated as can the wild-type enzyme. The active C174S mutant, however, could be inactivated by oxidation, and reactivated, but only by
reduction, not alternatively with high pH and high Mg2 + as is the case for the wild-type enzyme. In the sequence of Galdieria FBPase, the
Cys that corresponds to Cys179 in the spinach enzyme is lacking. However, the Galdieria FBPase, in contrast to the spinach Cys179 mutant,
does not show any indication for a comparable redox modulation of its activity. Instead, oxidation only leads to partial inactivation without
any qualitative changes in enzyme properties. Upon reduction, the lost activity can be recovered.
The corresponding mutants are active when expressed in E. coli, while C179S is inactive and can be reductivelyactivated as can the wild-type enzyme. The active C174S mutant, however, could be inactivated by oxidation, and reactivated, but only byreduction, not alternatively with high pH and high Mg2 + as is the case for the wild-type enzyme. In the sequence of Galdieria FBPase, theCys that corresponds to Cys179 in the spinach enzyme is lacking. However, the Galdieria FBPase, in contrast to the spinach Cys179 mutant,does not show any indication for a comparable redox modulation of its activity. Instead, oxidation only leads to partial inactivation withoutany qualitative changes in enzyme properties. Upon reduction, the lost activity can be recovered.
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