A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.

@article{Frlinger1998AMP,
  title={A multistep process is responsible for product-induced inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis.},
  author={M. F{\"u}rlinger and Dietmar Haltrich and Klaus D. Kulbe and Bernd Nidetzky},
  journal={European journal of biochemistry},
  year={1998},
  volume={251 3},
  pages={955-63}
}
Glucose-fructose oxidoreductase from the bacterium Zymomonas mobilis catalyzes a transhydrogenation reaction in which D-fructose reduction to D-sorbitol is coupled to the oxidation of D-glucose or other aldoses to the corresponding aldonolactones. Tightly protein-bound NADP(H) serves as the cofactor. We found that the interaction of glucose-fructose oxidoreductase with its aldonolactone product triggered a sequential process that affects the protein structure conformationally and chemically and… CONTINUE READING