Functional characteristics of the oxyanion hole in human acetylcholinesterase.

@article{Ordentlich1998FunctionalCO,
  title={Functional characteristics of the oxyanion hole in human acetylcholinesterase.},
  author={Arie Ordentlich and Dov Barak and Chanoch Kronman and Naomi Ariel and Yoffi Segall and Baruch Velan and Avigdor Shafferman},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 31},
  pages={19509-17}
}
The contribution of the oxyanion hole to the functional architecture and to the hydrolytic efficiency of human acetylcholinesterase (HuAChE) was investigated through single replacements of its elements, residues Gly-121, Gly-122 and the adjacent residue Gly-120, by alanine. All three substitutions resulted in about 100-fold decrease of the bimolecular rate constants for hydrolysis of acetylthiocholine; however, whereas replacements of Gly-120 and Gly-121 affected only the turnover number… CONTINUE READING