Molecular Origins of Selective Toxicity

Abstract

The major findings from the overall study are the following: Organophosphorus (OP) compounds recruit the full one-proton catalytic potential of acetylcholinesterase (AChE) in the course of the inhibition stage. AChE was found in the course of this research to be distinct from the serine proteases in possessing only a one-proton catalytic entity. The inhibition sequence for AChE and other serine hydrolases by OP agents involves not only the actual phosphorylation step ('chemical step') but also kinetically significant induced-fit steps ('physical step(s)'). Keywords: RA5; Serine hydrolase inhibition; Acetylcholinesterase organophosphates; Isotopic probes for acetylcholinesterase inhibition by organophosphates; Toxicity; Catalysis; Serine protease; Enzymes.

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Document Details

Document Type
Technical Report
Publication Date
Nov 01, 1987
Accession Number
ADA219667

Entities

People

  • Ildiko M. Kovach
  • Richard L. Schowen

Organizations

  • University of Kansas

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Biomedical Research
  • Chemical Reaction Properties
  • Chemical Reactions
  • Chemical Synthesis
  • Chemistry
  • Enzyme Inhibitors
  • Ethers
  • Heavy Water
  • Measurement
  • Organic Chemistry

Readers

  • Molecular and Cellular Biochemistry
  • Neurotoxicology