Allosteric properties, substrate specificity, and subsite affinities of honeybee alpha-glucosidase I.

@article{Kimura1990AllostericPS,
  title={Allosteric properties, substrate specificity, and subsite affinities of honeybee alpha-glucosidase I.},
  author={Atsuomi Kimura and Shun-ichi Takewaki and Hiroshi Matsui and Minoru Kubota and Shingo Chiba},
  journal={Journal of biochemistry},
  year={1990},
  volume={107 5},
  pages={
          762-8
        }
}
The substrate specificity of honeybee alpha-glucosidase I, a monomeric enzyme was kinetically investigated. Unusual kinetic features were observed in the cleavage reactions of sucrose, maltose, p-nitrophenyl alpha-glucoside, phenyl alpha-glucoside, turanose, and maltodextrin (DP = 13). At relatively high substrate concentrations, the velocities of liberation of fructose from sucrose, glucose from maltose, p-nitrophenol from p-nitrophenyl alpha-glucoside, and phenol from phenyl alpha-glucoside… CONTINUE READING

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