Inactivation of Electrophorus electricus acetylcholinesterase by benzenemethane sulfonylfluoride

Philip Barnett, Terrone L. Rosenberry

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Benzenemethane Sulfonylfluoride (329-98-6) is an irreversible inactivator of many esterases including mammalian acetylcholinesterases. However, previous reports indicated that acetylcholinesterase from the electric eel, Electrophorus electricus (EC 3.1.1.7) failed to react with benzenemethane sulfonylfluoride at measurable rates. We report here that eel acetylcholinesterase reacts with this inactivator at a low rate. Hydrolysis of the sulfonylating agent is so much faster than enzyme inactivation that, under most conditions, there will be only slight inactivation. Like the reaction of other active site acylating agents with this enzyme, inactivation can be accelerated in the presence of certain organic cations. We introduce a rate equation for enzyme sulfonylation which incorporates both the hydrolysis of the inactivator and the complication that fluoride resulting from hydrolysis of the inactivator is a potent competitive inhibitor of this enzyme. This rate equation accurately describes the time course of enzyme inactivation.

Original languageEnglish (US)
Pages (from-to)202-205
Number of pages4
JournalArchives of Biochemistry and Biophysics
Volume190
Issue number1
DOIs
StatePublished - 1978
Externally publishedYes

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Electrophorus
Acetylcholinesterase
Hydrolysis
Enzymes
Eels
Enzyme Inhibitors
Esterases
Fluorides
Cations
Catalytic Domain

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Inactivation of Electrophorus electricus acetylcholinesterase by benzenemethane sulfonylfluoride. / Barnett, Philip; Rosenberry, Terrone L.

In: Archives of Biochemistry and Biophysics, Vol. 190, No. 1, 1978, p. 202-205.

Research output: Contribution to journalArticle

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