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Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Enzymes

  • Rohit Medhekar
  • Nathan Baker
  • Kenneth Sando
  • William Kearney
  • Daniel Quinn

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.

Keywords

Catalytic Activity Potential Energy Proton Transfer Point Charge Nucleophilic Attack 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Rohit Medhekar
    • 1
  • Nathan Baker
    • 2
  • Kenneth Sando
    • 1
  • William Kearney
    • 1
  • Daniel Quinn
    • 1
  1. 1.Department of ChemistryThe University of IowaIowa CityUSA
  2. 2.Department of PharmacologyUniversity of California at San DiegoLa JollaUSA

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