Abstract
Acetylcholinesterase (AChE) and chymotrypsin are serine enzymes whose catalytic mechanism involves a nucleophilic attack (serine) and a general acid-base moiety (histidine). The incipient imidiazolium which is formed as a result of the nucleophilic attack by serine is stabilized by the negatively charged carboxylate (Glu or Asp). This transition state stabilization is thought to be gained by a low-barrier hydrogen bond (LBHB) in which the proton is centrally located between N5 and the carboxylate oxygen.
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© 1998 Springer Science+Business Media New York
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Medhekar, R., Baker, N., Sando, K., Kearney, W., Quinn, D. (1998). Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Enzymes. In: Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. (eds) Structure and Function of Cholinesterases and Related Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1540-5_62
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DOI: https://doi.org/10.1007/978-1-4899-1540-5_62
Publisher Name: Springer, Boston, MA
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