RESEARCH ARTICLE


Kitz-Wilson Mechanisms of Action of Neostigmine and Penicillin



T.A. Alston*
Department of Anesthesia and Critical Care, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA.


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Creative Commons License
Alston et al.; Licensee Bentham Open

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the Department of Anesthesia and Critical Care, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA; E-mail: talston@partners.org


Abstract

The molecular mechanism of penicillin action is closely analogous to that of neostigmine. Both drugs react covalently with the active-site serine of their target enzymes. In both cases, the susceptible enzymes self-catalyze their inactivation by their respective drugs. Kinetic analysis of cholinesterase by Richard J. Kitz and Irwin B. Wilson helped to establish that concept. Neostigmine and penicillin are kindred examples of mechanism-based enzyme inhibition, a generally important phenomenon in pharmacology and physiology.