TY - JOUR
T1 - Is acetyl/butyrylcholine specificity a marker for insecticide-resistance mutations in insect acetylcholinesterase?
AU - Kim, Beom Seok
AU - Lee, Jung Yeop
AU - Hwang, Byung Kook
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
KW - Acetyl/butyrylthiocholine
KW - Acetylcholinesterase
KW - Insect
KW - Insecticide resistance
KW - Mutation
KW - Resistance
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U2 - 10.1002/1526-4998(200012)56:12<1023::AID-PS240>3.0.CO;2-I
DO - 10.1002/1526-4998(200012)56:12<1023::AID-PS240>3.0.CO;2-I
M3 - Article
AN - SCOPUS:0033660683
VL - 56
SP - 1023
EP - 1028
JO - Pest Management Science
JF - Pest Management Science
SN - 1526-498X
IS - 12
ER -