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 language | English |
|---|---|
| Pages (from-to) | 1023-1028 |
| Number of pages | 6 |
| Journal | Pest Management Science |
| Volume | 56 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 2000 Dec 16 |
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Keywords
- Acetyl/butyrylthiocholine
- Acetylcholinesterase
- Insect
- Insecticide resistance
- Mutation
- Resistance
ASJC Scopus subject areas
- Agronomy and Crop Science
- Insect Science
Cite this
Is acetyl/butyrylcholine specificity a marker for insecticide-resistance mutations in insect acetylcholinesterase? / Kim, Beom Seok; Lee, Jung Yeop; Hwang, Byung Kook.
In: Pest Management Science, Vol. 56, No. 12, 16.12.2000, p. 1023-1028.Research output: Contribution to journal › Article
}
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 - 2000/12/16
Y1 - 2000/12/16
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
UR - http://www.scopus.com/inward/record.url?scp=0033660683&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033660683&partnerID=8YFLogxK
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 -