Purification and characterization of a carboxylesterase involved in insecticide resistance from the mosquito Culex quinquefasciatus

A. J. Ketterman; K. G.I. Jayawardena; Janet Hemingway

doi:10.1042/bj2870355

Purification and characterization of a carboxylesterase involved in insecticide resistance from the mosquito Culex quinquefasciatus

A. J. Ketterman, K. G.I. Jayawardena, Janet Hemingway

London School of Hygiene and Tropical Medicine

Research output: Contribution to journal › Article › peer-review

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Abstract

A carboxylesterase (EC 3.1.1.1) involved in organophosphate insecticide resistance has been purified and characterized from the mosquito Culex quinquefasciatus. The monomeric enzyme has M(r) of 67000 and a pl of 5.2. It hydrolysed medium-chain-length mono- and di-acylglycerols in addition to xenobiotic esters. Kinetic constants determined for four insecticides, temephos, chlorpyrifos, fenitrothion and propoxur indicate the rates of acylation and the affinities of binding of the insecticides to this carboxylesterase are important. This supports the major role of the A2 carboxylesterase is the sequestration of the insecticide with a minor role in the slow turnover of the insecticide.

Original language	English
Pages (from-to)	355-360
Number of pages	6
Journal	Biochemical Journal
Volume	287
Issue number	2
DOIs	https://doi.org/10.1042/bj2870355
Publication status	Published - 1 Jan 1992
Externally published	Yes

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title = "Purification and characterization of a carboxylesterase involved in insecticide resistance from the mosquito Culex quinquefasciatus",

abstract = "A carboxylesterase (EC 3.1.1.1) involved in organophosphate insecticide resistance has been purified and characterized from the mosquito Culex quinquefasciatus. The monomeric enzyme has M(r) of 67000 and a pl of 5.2. It hydrolysed medium-chain-length mono- and di-acylglycerols in addition to xenobiotic esters. Kinetic constants determined for four insecticides, temephos, chlorpyrifos, fenitrothion and propoxur indicate the rates of acylation and the affinities of binding of the insecticides to this carboxylesterase are important. This supports the major role of the A2 carboxylesterase is the sequestration of the insecticide with a minor role in the slow turnover of the insecticide.",

author = "Ketterman, \{A. J.\} and Jayawardena, \{K. G.I.\} and Janet Hemingway",

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T1 - Purification and characterization of a carboxylesterase involved in insecticide resistance from the mosquito Culex quinquefasciatus

AU - Ketterman, A. J.

AU - Jayawardena, K. G.I.

AU - Hemingway, Janet

PY - 1992/1/1

Y1 - 1992/1/1

N2 - A carboxylesterase (EC 3.1.1.1) involved in organophosphate insecticide resistance has been purified and characterized from the mosquito Culex quinquefasciatus. The monomeric enzyme has M(r) of 67000 and a pl of 5.2. It hydrolysed medium-chain-length mono- and di-acylglycerols in addition to xenobiotic esters. Kinetic constants determined for four insecticides, temephos, chlorpyrifos, fenitrothion and propoxur indicate the rates of acylation and the affinities of binding of the insecticides to this carboxylesterase are important. This supports the major role of the A2 carboxylesterase is the sequestration of the insecticide with a minor role in the slow turnover of the insecticide.

AB - A carboxylesterase (EC 3.1.1.1) involved in organophosphate insecticide resistance has been purified and characterized from the mosquito Culex quinquefasciatus. The monomeric enzyme has M(r) of 67000 and a pl of 5.2. It hydrolysed medium-chain-length mono- and di-acylglycerols in addition to xenobiotic esters. Kinetic constants determined for four insecticides, temephos, chlorpyrifos, fenitrothion and propoxur indicate the rates of acylation and the affinities of binding of the insecticides to this carboxylesterase are important. This supports the major role of the A2 carboxylesterase is the sequestration of the insecticide with a minor role in the slow turnover of the insecticide.

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DO - 10.1042/bj2870355

M3 - Article

SN - 0264-6021

VL - 287

SP - 355

EP - 360

JO - Biochemical Journal

JF - Biochemical Journal

IS - 2

ER -

Purification and characterization of a carboxylesterase involved in insecticide resistance from the mosquito Culex quinquefasciatus

Abstract

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