Is acetyl/butyrylcholine specificity a marker for insecticide-resistance mutations in insect acetylcholinesterase?

Beom Seok Kim, Jung Yeop Lee, Byung Kook Hwang

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

Substrate specificity has been widely studied in vertebrate cholinesterases and it has been shown that two phenylalanines in the acyl pocket of acetylcholinesterase govern the acceptance of the acetyl/butyryl moiety of the choline esters. As an insecticide-resistance mutation has been evidenced in the acyl pocket of Drosophila melanogaster and Musca domestica acetylcholinesterase we investigated the possibility of linking changes in acetyl/butyrylthiocholine specificity with mutations in insect acetylcholinesterase. We thus analyzed the effect of 28 mutations in Drosophila enzyme on acetyl/butyrylthiocholine, N-methyl/N-propyl-carbamates and ethyl/methyl-paraoxon preference. It appeared that the highest changes on acetyl/butyrylthiocholine and N-propyl/N-methyl-carbamates preference were due to mutations in the acyl pocket. Nevertheless, other insecticide-resistance mutations, not located in the acyl pockets also modified these substrate preferences. Moreover, the effect of mutations in the acyl pocket was hidden when some other insecticide-resistance mutations were combined in the enzyme. Consequently, acetyl/butyrylthiocholine preference alteration cannot be used as a marker to localize a mutation in the insect ACHE. (C) 2000 Society of Chemical Industry.

Original languageEnglish
Pages (from-to)1023-1028
Number of pages6
JournalPest Management Science
Volume56
Issue number12
DOIs
Publication statusPublished - 2000

Keywords

  • Acetyl/butyrylthiocholine
  • Acetylcholinesterase
  • Insect
  • Insecticide resistance
  • Mutation
  • Resistance

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Insect Science

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