Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts.

@article{Li2005AcarboseRM,
  title={Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts.},
  author={Chunmin Li and A. Sabeena Begum and Shin Numao and Kwan Hwa Park and Stephen G Withers and Gary D. Brayer},
  journal={Biochemistry},
  year={2005},
  volume={44 9},
  pages={3347-57}
}
A mechanistic study of the poorly understood pathway by which the inhibitor acarbose is enzymatically rearranged by human pancreatic alpha-amylase has been conducted by structurally examining the binding modes of the related inhibitors isoacarbose and acarviosine-glucose, and by novel kinetic measurements of all three inhibitors under conditions that demonstrate this rearrangement process. Unlike acarbose, isoacarbose has a unique terminal alpha-(1-6) linkage to glucose and is found to be… CONTINUE READING