메뉴 건너뛰기




Volumn 37, Issue 9, 2007, Pages 891-902

Hydrolysis of individual isomers of fluorogenic pyrethroid analogs by mutant carboxylesterases from Lucilia cuprina

Author keywords

Esterases; In vitro mutagenesis; Insecticide; Isomers; Pyrethroid hydrolase; Resistance

Indexed keywords

CARBOXYLESTERASE; PYRETHROID;

EID: 34547538215     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2007.04.011     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0017884187 scopus 로고
    • Syntheses of diastereoisomers of the recent pyrethroids, fenvalerate (S-5602) and cypermethrin (NRDC-149) from (-)-3-phenoxy-mandelic acid and determination of their absolute configurations
    • Aketa K.-I., Ohno N., Itaya N., Nakayama I., and Yoshioka H. Syntheses of diastereoisomers of the recent pyrethroids, fenvalerate (S-5602) and cypermethrin (NRDC-149) from (-)-3-phenoxy-mandelic acid and determination of their absolute configurations. Agric. Biol. Chem. 42 (1978) 895-896
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 895-896
    • Aketa, K.-I.1    Ohno, N.2    Itaya, N.3    Nakayama, I.4    Yoshioka, H.5
  • 3
    • 34248143941 scopus 로고
    • *), 2 α] } - 2 - (2, 2 - dichlorovinyl) - 3, 3 - dimethylcyclopropanecarboxylic acid cyano(3-phenoxyphenyl)methyl ester (RU 24501)
    • *), 2 α] } - 2 - (2, 2 - dichlorovinyl) - 3, 3 - dimethylcyclopropanecarboxylic acid cyano(3-phenoxyphenyl)methyl ester (RU 24501). Acta Crystallogr., Sect. C 47 (1991) 606-608
    • (1991) Acta Crystallogr., Sect. C , vol.47 , pp. 606-608
    • Baert, F.1    Guelzim, A.2
  • 4
    • 0032029864 scopus 로고    scopus 로고
    • Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina
    • Campbell P.M., Newcomb R.D., Russell R.J., and Oakeshott J.G. Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina. Insect Biochem. Mol. Biol. 28 (1998) 139-150
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 139-150
    • Campbell, P.M.1    Newcomb, R.D.2    Russell, R.J.3    Oakeshott, J.G.4
  • 6
    • 34547526943 scopus 로고    scopus 로고
    • Claudianos, C., 1999. The evolution of α-esterase mediated organophosphate resistance in Musca domestica. Ph.D. Thesis, Australian National University.
  • 7
    • 0033179577 scopus 로고    scopus 로고
    • The same amino acid substitution in orthologous esterases confers organophosphate resistance on the house fly and a blowfly
    • Claudianos C., Russell R.J., and Oakeshott J.G. The same amino acid substitution in orthologous esterases confers organophosphate resistance on the house fly and a blowfly. Insect Biochem. Molec. Biol. 29 (1999) 675-686
    • (1999) Insect Biochem. Molec. Biol. , vol.29 , pp. 675-686
    • Claudianos, C.1    Russell, R.J.2    Oakeshott, J.G.3
  • 8
    • 0013137142 scopus 로고    scopus 로고
    • A genomics perspective on mutant aliesterases and metabolic resistance to organophosphates
    • Clark J.M., and Yamaguchi I. (Eds), ACS Symposium Series 808, American Chemical Society, Washington
    • Claudianos C., Crone E.J., Coppin C., Russell R.J., and Oakeshott J.G. A genomics perspective on mutant aliesterases and metabolic resistance to organophosphates. In: Clark J.M., and Yamaguchi I. (Eds). Agrochemical Resistance: Extent, Mechanism and Detection (2001), ACS Symposium Series 808, American Chemical Society, Washington 90-101
    • (2001) Agrochemical Resistance: Extent, Mechanism and Detection , pp. 90-101
    • Claudianos, C.1    Crone, E.J.2    Coppin, C.3    Russell, R.J.4    Oakeshott, J.G.5
  • 10
    • 33750725686 scopus 로고    scopus 로고
    • A survey of mutations in the Cochliomyia hominivorax (Diptera: Calliphoridae) esterase E3 gene associated with organophosphate resistance and the molecular identification of mutant alleles
    • de Carvalho R.A., Torres T.T., and de Azeredo-Espin A.M.L. A survey of mutations in the Cochliomyia hominivorax (Diptera: Calliphoridae) esterase E3 gene associated with organophosphate resistance and the molecular identification of mutant alleles. Vet. Parasitol. 140 (2006) 344-351
    • (2006) Vet. Parasitol. , vol.140 , pp. 344-351
    • de Carvalho, R.A.1    Torres, T.T.2    de Azeredo-Espin, A.M.L.3
  • 11
    • 0020382756 scopus 로고
    • A carboxylesterase with broad substrate specificity causes organophosphorus, carbamate and pyrethroid resistance in peach-potato aphids (Myzus persicae)
    • Devonshire A.L., and Moores G.D. A carboxylesterase with broad substrate specificity causes organophosphorus, carbamate and pyrethroid resistance in peach-potato aphids (Myzus persicae). Pestic. Biochem. Physiol. 18 (1982) 235-246
    • (1982) Pestic. Biochem. Physiol. , vol.18 , pp. 235-246
    • Devonshire, A.L.1    Moores, G.D.2
  • 13
    • 37049105753 scopus 로고
    • Synthetic pyrethroids-a new class of insecticide
    • Elliott M., and Janes N.F. Synthetic pyrethroids-a new class of insecticide. Chem. Soc. Rev. 7 (1978) 473-505
    • (1978) Chem. Soc. Rev. , vol.7 , pp. 473-505
    • Elliott, M.1    Janes, N.F.2
  • 14
    • 0027182474 scopus 로고
    • Cloning and analysis of the esterase genes conferring insecticide resistance in the peach-potato aphid Myzus persicae (Sulzer)
    • Field L.M., Williamson M.S., Moores G.D., and Devonshire A.L. Cloning and analysis of the esterase genes conferring insecticide resistance in the peach-potato aphid Myzus persicae (Sulzer). Biochem. J. 294 (1993) 569-574
    • (1993) Biochem. J. , vol.294 , pp. 569-574
    • Field, L.M.1    Williamson, M.S.2    Moores, G.D.3    Devonshire, A.L.4
  • 18
    • 17844391590 scopus 로고    scopus 로고
    • Hydrolysis of pyrethroids by carboxylesterases from Lucilia cuprina and Drosophila melanogaster with active sites modified by in vitro mutagenesis
    • Heidari R., Devonshire A.L., Campbell B.E., Dorrian S.J., Oakeshott J.G., and Russell R.J. Hydrolysis of pyrethroids by carboxylesterases from Lucilia cuprina and Drosophila melanogaster with active sites modified by in vitro mutagenesis. Insect Biochem. Mol. Biol. 35 (2005) 597-609
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 597-609
    • Heidari, R.1    Devonshire, A.L.2    Campbell, B.E.3    Dorrian, S.J.4    Oakeshott, J.G.5    Russell, R.J.6
  • 19
    • 15344341737 scopus 로고    scopus 로고
    • Development of optically pure pyrethroid-like fluorescent substrates for carboxylesterases
    • Huang H., Stok J.E., Stoutamire D.W., Gee S.J., and Hammock B.D. Development of optically pure pyrethroid-like fluorescent substrates for carboxylesterases. Chem. Res. Toxicol. 18 (2005) 516-527
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 516-527
    • Huang, H.1    Stok, J.E.2    Stoutamire, D.W.3    Gee, S.J.4    Hammock, B.D.5
  • 20
    • 25444494162 scopus 로고    scopus 로고
    • Stereoselective hydrolysis of pyrethroid-like fluorescent substrates by human and other mammalian liver carboxylesterases
    • Huang H., Fleming C.D., Nishi K., Redinbo M.R., and Hammock B.D. Stereoselective hydrolysis of pyrethroid-like fluorescent substrates by human and other mammalian liver carboxylesterases. Chem. Res. Toxicol. 18 (2005) 1371-1377
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1371-1377
    • Huang, H.1    Fleming, C.D.2    Nishi, K.3    Redinbo, M.R.4    Hammock, B.D.5
  • 21
    • 0021708080 scopus 로고
    • Stereochemical aspects of cholinesterase catalysis
    • Järv J. Stereochemical aspects of cholinesterase catalysis. Bioorg. Chem. 12 (1984) 259-278
    • (1984) Bioorg. Chem. , vol.12 , pp. 259-278
    • Järv, J.1
  • 22
    • 0034681279 scopus 로고    scopus 로고
    • Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica
    • Koellner G., Kryger G., Millard C.B., Silman I., Sussman J.L., and Steiner T. Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica. J. Mol. Biol. 296 (2000) 713-735
    • (2000) J. Mol. Biol. , vol.296 , pp. 713-735
    • Koellner, G.1    Kryger, G.2    Millard, C.B.3    Silman, I.4    Sussman, J.L.5    Steiner, T.6
  • 24
    • 0030612598 scopus 로고    scopus 로고
    • A single amino acid substitution converts a carboxylesterase to an organophosphorous hydrolase and confers insecticide resistance on a blowfly
    • Newcomb R.D., Campbell P.M., Ollis D.L., Cheah E., Russell R.J., and Oakeshott J.G. A single amino acid substitution converts a carboxylesterase to an organophosphorous hydrolase and confers insecticide resistance on a blowfly. Proc. Natl. Acad. Sci. USA 94 (1997) 7464-7468
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7464-7468
    • Newcomb, R.D.1    Campbell, P.M.2    Ollis, D.L.3    Cheah, E.4    Russell, R.J.5    Oakeshott, J.G.6
  • 28
    • 0026794595 scopus 로고
    • Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants
    • Radic Z., Gibney G., Kawamoto S., MacPhee-Quigley S., Bongiorno C., and Taylor P. Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants. Biochem. 31 (1992) 9760-9767
    • (1992) Biochem. , vol.31 , pp. 9760-9767
    • Radic, Z.1    Gibney, G.2    Kawamoto, S.3    MacPhee-Quigley, S.4    Bongiorno, C.5    Taylor, P.6
  • 29
    • 0027336654 scopus 로고
    • 1.8 Å refined structure of the lipase from Geotrichum candidum
    • Schrag J.D., and Cygler M. 1.8 Å refined structure of the lipase from Geotrichum candidum. J. Mol. Biol. 230 (1993) 575-591
    • (1993) J. Mol. Biol. , vol.230 , pp. 575-591
    • Schrag, J.D.1    Cygler, M.2
  • 30
    • 0035576898 scopus 로고    scopus 로고
    • Development of sensitive esterase assays based on α-cyano-containing esters
    • Shan G., and Hammock B.D. Development of sensitive esterase assays based on α-cyano-containing esters. Anal. Biochem. 299 (2001) 54-62
    • (2001) Anal. Biochem. , vol.299 , pp. 54-62
    • Shan, G.1    Hammock, B.D.2
  • 31
    • 3142676638 scopus 로고    scopus 로고
    • Identification, expression, and purification of a pyrethroidhydrolyzing carboxylesterase from mouse liver microsomes
    • Stok J.E., Huang H., Jones P.D., Wheelock C.E., Morisseau C., and Hammock B.D. Identification, expression, and purification of a pyrethroidhydrolyzing carboxylesterase from mouse liver microsomes. J. Biol. Chem. 279 (2004) 29863-29869
    • (2004) J. Biol. Chem. , vol.279 , pp. 29863-29869
    • Stok, J.E.1    Huang, H.2    Jones, P.D.3    Wheelock, C.E.4    Morisseau, C.5    Hammock, B.D.6
  • 32
    • 9444285821 scopus 로고    scopus 로고
    • Determination of malathion and diazinon resistance by sequencing the Md α E 7 gene from Guatemala, Columbia, Manhattan and Thailand housefly (Musca domestica L.)
    • Taskin V., Kence M., and Göçmen B. Determination of malathion and diazinon resistance by sequencing the Md α E 7 gene from Guatemala, Columbia, Manhattan and Thailand housefly (Musca domestica L.). strains. Russ. J. Genet. 40 (2004) 377-380
    • (2004) strains. Russ. J. Genet. , vol.40 , pp. 377-380
    • Taskin, V.1    Kence, M.2    Göçmen, B.3
  • 33
    • 0002155659 scopus 로고
    • Organophosphate resistance and esterase activity in houseflies
    • van Asperen K., and Oppenoorth F.J. Organophosphate resistance and esterase activity in houseflies. Entomol. Exper. Applic. 2 (1959) 48-57
    • (1959) Entomol. Exper. Applic. , vol.2 , pp. 48-57
    • van Asperen, K.1    Oppenoorth, F.J.2
  • 34
    • 0032971320 scopus 로고    scopus 로고
    • Detection of single-base substitution in an esterase gene and its linkage to malathion resistance in the parasitoid Anisopteromalus calandrae (Hymenoptera: Pteromalidae)
    • Zhu Y.C., Dowdy A.K., and Baker J.E. Detection of single-base substitution in an esterase gene and its linkage to malathion resistance in the parasitoid Anisopteromalus calandrae (Hymenoptera: Pteromalidae). Pestic. Sci. 55 (1999) 398-404
    • (1999) Pestic. Sci. , vol.55 , pp. 398-404
    • Zhu, Y.C.1    Dowdy, A.K.2    Baker, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.