UDP-glucose pyrophosphorylase from potato tuber: purification and characterization.

  title={UDP-glucose pyrophosphorylase from potato tuber: purification and characterization.},
  author={Kengo Nakano and Yuri Omura and Mitsuo Tagaya and Toshio Fukui},
  journal={Journal of biochemistry},
  volume={106 3},
UDP-glucose pyrophosphorylase from potato tuber was purified 243-fold to a nearly homogeneous state with a recovery of 30%. The purified enzyme utilized UDP-glucose, but not ADP-glucose, as the substrate, and was not activated by 3-phosphoglyceric acid. Product inhibition studies revealed the sequential binding of UDP-glucose and MgPPi and the sequential release of glucose-1-phosphate and MgUTP, in this order. Analyses of the effects of Mg2+ on the enzyme activity suggest that the MgPPi and… CONTINUE READING