55667-40-8Relevant articles and documents
Chapman,Harris
, p. 369,373 (1979)
EFFECT OF MOLECULAR STRUCTURE ON STEREOSELECTIVITY DURING THE HYDROLYSIS OF DIASTEREOISOMERIC PERMETHRINIC ACID ESTERS
Simon, Kalmal,Boros, Iren,Balogh, Gyula,Hidasi, Gyeorgy,Fogassy, Elemer,et al.
, p. 111 - 124 (1987)
Chemical behaviour and thermal stability differences between the diastereoisomeric cis- and trans-permethrines are elucidated on the basis of their crystal structures.Crystals of the trans-isomer are monoclinic with space group C2/c, with 8 molecules in a unit cell of dimensions a = 38.030(5), b = 9.163(2), c = 11.715(6) Angstroem and B = 105.95(4).Previously published cis-structures are reinvestigated in order to obtain the same accoracy for both derivatives.
Molecular cloning, purification, and biochemical characterization of a novel pyrethroid-hydrolyzing esterase from Klebsiella sp. strain ZD112
Wu, Pei C.,Liu, Yu H.,Wang, Zhuo Y.,Zhang, Xiao Y.,Li, He,Liang, Wei Q.,Luo, Na,Hu, Ji M.,Lu, Jia Q.,Luan, Tian G.,Cao, Li X.
, p. 836 - 842 (2007/10/03)
The gene encoding pyrethroid-hydrolyzing esterase (EstP) from Klebsiella sp. strain ZD112 was cloned into Escherichia coli and sequenced. A sequence analysis of the DNA responsible for the esfP gene revealed an open reading frame of 1914 bp encoding for a protein of 637 amino acid residues. No similarities were found by a database homology search using the nucleotide and deduced amino acid sequences of the esterases and lipases. EstP was heterologously expressed in E. coli and purified. The molecular mass of the native enzyme was approximately 73 kDa as determined by gel filtration. The results of sodium dodecyl sulfate - polyacrylamide gel electrophoresis and the deduced amino acid sequence of EstP indicated molecular masses of 73 and 73.5 kDa, respectively, suggesting that EstP is a monomer. The purified EstP not only degraded many pyrethroid pesticides and the organophosphorus insecticide malathion, but also hydrolyzed ρ-nitrophenyl esters of various fatty acids, indicating that EstP is an esterase with broad substrates. The Km for trans- and cis-permethrin and kcat/Km values indicate that EstP hydrolyzes both these substrates with higher efficiency than the carboxylesterases from resistant insects and mammals. The catalytic activity of EstP was strongly inhibited by Hg2+, Ag+, and ρ-chloromercuribenzoate, whereas a less pronounced effect (3-8% inhibition) was observed in the presence of divalent cations, the chelating agent EDTA, and phenanthroline.
Development of pyrethroid substrates for esterases associated with pyrethroid resistance in the tobacco budworm, Heliothis virescens (F.)
Huang, Huazhang,Ottea, James A.
, p. 6539 - 6545 (2007/10/03)
Assays to detect esterases associated with resistance to organophosphorus and pyrethroid insecticides in larvae of H. virescens were developed and evaluated. Cross-resistance to a variety of insecticides was measured in strains resulting from selection with either profenofos (OP-R) or cypermethrin (PYR-R), and resistance in both strains appeared to have a metabolic component. Esters were synthesized that coupled 3-(2,2-dichlorovinyl)-2,2- dimethylcyclopropanecarboxylate, the acid moiety of some pyrethroid insecticides, with groups (e.g., p-nitrophenyl-) that could be detected spectrophotometrically following hydrolysis of the resulting esters. Activities toward these pyrethroid esters were significantly higher in both resistant strains than those in a susceptible reference strain. In addition, all pyrethroid esters significantly increased the toxicity of cypermethrin in bioassays with larvae from both PYR-R and OP-R strains. The biological and biochemical activities of these compounds are compared with those with more conventional esterase substrates and insecticide synergists, and the utility of pyrethroid esters as components of rapid assays for detecting esterases associated with insecticide resistance is discussed.
