Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase.

@article{Masson1997RoleOA,
  title={Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase.},
  author={Patrick Masson and Pierre Legrand and Cynthia F Bartels and Marie Th{\'e}r{\`e}se Froment and Lawrence M Schopfer and Oksana Lockridge},
  journal={Biochemistry},
  year={1997},
  volume={36 8},
  pages={
          2266-77
        }
}
The atypical variant of human butyrylcholinesterase has Gly in place of Asp 70. Patients with this D70G mutation respond abnormally to the muscle relaxant succinyldicholine, experiencing hours of apnea rather than the intended 3 min. Asp 70 is at the rim of the active site gorge 12 A from the active site Ser 198. An unanswered question in the literature is why the atypical variant has a 10-fold increase in Km for compounds with a single positive charge but a 100-fold increase in Km for… CONTINUE READING
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