Nonoxidative Enzymes in the Metabolism of Insecticides

Ahmad, Sami; Forgash, Andrew J.

doi:10.3109/03602537608995840

Cited by 57 publications

(36 citation statements)

References 85 publications

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“…aegypti resistance to organophosphates in the Caribbean linked to elevate carboxylesterases activities have been described (Rodriguez et al 2001;Marcombe et al 2009). Carboxylesterases are also implicated in the metabolism of exogenous substrates (i.e., insecticides) (Ahmad and Forgash 1976;Kapin and Ahmad 1980). Hence, the present study was made to analyse the chemical constituents and to study the anti-dengue activity of P. nigrum leaf compounds identified through biochemical and histopathological changes against the larvae of Ae.…”

Section: Introductionmentioning

confidence: 99%

Physiological and biochemical effects of botanical extract from Piper nigrum Linn (Piperaceae) against the dengue vector Aedes aegypti Liston (Diptera: Culicidae)

et al. 2015

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The leaves of Piper nigrum L. (Piperaceae) were evaluated for chemical constituents and mosquito larvicidal activity against the larvae of Aedes aegypti. GC and GC-MS analyses revealed that the crude extracts contain 16 compounds. Thymol (20.77%) and ç-elemene (10.42%) were identified as the major constituents followed by cyclohexene, 4-ethenyl-4-methyl-3-(1-methylethenyl)-1-(1 methylethyl)-, (3R-trans) (7.58%), 4,6-octadienoic acid, 2-acetyl-2-methyl-, ethyl ester (6.98), 2(3H)-furanone, 3,4-bis(1,3-benzodioxol-5-ylmethyl) dihydro-, (3R-trans) (6.95%), 1-naphthalenol, 1,2,3,4,4a,7,8,8a-octahydro-1,6-dimethyl-4-(1-methylethyl)-, [1R-(1à,4á,4aá,8aá)]-(Cedreanol) (5.30%), trans-2-undecen-1-ol (4.48%), phytol (4.22%), 1,6-cyclodecadiene, 1-methyl-5-methylene-8-(1-methylethyl)-,[s-(E,E)] (3.78%) and 2,6-dimethyl-3,5,7-octatriene-2-ol, Z,Z (2.39%). Larval mortality was observed after 3 h of exposure period. The crude extract showed remarkable larvicidal activity against Ae. aegypti (LC50 = 34.97). The larvae of Ae. aegypti exposed to the P. nigrum, significantly reduced the activities of α- and β-carboxylesterases and superdioxide. Further, P. nigrum extract was severely affecting the mosquito gut cellular organelles. Based on the results, the chemical constituents of crude extracts of P. nigrum can be considered as a new source of larvicide for the control of Ae. aegypti.

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Section: Introductionmentioning

confidence: 99%

Physiological and biochemical effects of botanical extract from Piper nigrum Linn (Piperaceae) against the dengue vector Aedes aegypti Liston (Diptera: Culicidae)

et al. 2015

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“…They share a characteristic α/β-hydrolase structure, including a catalytic triad composed of Ser-Glu (Asp)-His and the nucleophilic elbow surrounding the active-site serine residue (GXSXG) (Oakeshott et al, 1999). Mammalian CarEs play an important role in biotransformation of many drugs (Imai, 2006) and transesterification of xenobiotics such as insecticides (Ahmad and Forgash, 1976).…”

Section: Introductionmentioning

confidence: 99%

RNA interference revealed the roles of two carboxylesterase genes in insecticide detoxification in Locusta migratoria

Zhang

et al. 2013

Chemosphere

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Carboxylesterases (CarEs) play key roles in metabolism of specific hormones and detoxification of dietary and environmental xenobiotics in insects. We sequenced and characterized CarE cDNAs putatively derived from two different genes named LmCesA1 and LmCesA2 from the migratory locust, Locusta migratoria, one of the most important agricultural pests in the world. The full-length cDNAs of LmCesA1 (1892 bp) and LmCesA2 (1643 bp) encode 543 and 501 amino acid residues, respectively. The two deduced CarEs share a characteristic α/β-hydrolase structure, including a catalytic triad composed of Ser-Glu (Asp)-His and a consensus sequence GQSAG, which suggests that both CarEs are biologically active. Phylogenetic analysis grouped both LmCesA1 and LmCesA2 into clade A which has been suggested to be involved in dietary detoxification. Both transcripts were highly expressed in all the nymphal and adult stages, but only slightly expressed in eggs. Analyses of tissue-dependent expression and in situ hybridization revealed that both transcripts were primarily expressed in gastric caeca. RNA interference (RNAi) of LmCesA1 and LmCesA2 followed by a topical application of carbaryl or deltamethrin did not lead to a significantly increased mortality with either insecticide. However, RNAi of LmCesA1 and LmCesA2 increased insect mortalities by 20.9 and 14.5%, respectively, when chlorpyrifos was applied.These results suggest that these genes might not play a significantly role in detoxification of carbaryl and deltamethrin but are most likely to be involved in detoxification of chlorpyrifos in L. migratoria.3

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“…[1][2][3][4][5][6][7][8][9] The enzyme utilizes a standard two-step hydrolase mechanism in which the catalytic serine is activated for nucleophilic attack by adjacent histidine and glutamic acid residues in a catalytic triad. The acyl-enzyme intermediate formed between the serine and a portion of the substrate is released in the second step of the reaction either by an attacking water molecule (hydrolysis) or by an abundant alcohol (transesterification).…”

Section: Introductionmentioning

confidence: 99%

Multisite Promiscuity in the Processing of Endogenous Substrates by Human Carboxylesterase 1

Bencharit

Edwards

Morton

et al. 2006

Journal of Molecular Biology

130

141

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Human carboxylesterase 1 (hCE1) is a drug and endobiotic-processing serine hydrolase that exhibits relatively broad substrate specificity. It has been implicated in a variety of endogenous cholesterol metabolism pathways including the following apparently disparate reactions: cholesterol ester hydrolysis (CEH), fatty acyl Coenzyme A hydrolysis (FACoAH), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES). The structural basis for the ability of hCE1 to perform these catalytic actions involving large substrates and products has remained unclear. Here we present four crystal structures of the hCE1 glycoprotein in complexes with the following endogenous substrates or substrate analogues: Coenzyme A, the fatty acid palmitate, and the bile acids cholate and taurocholate. While the active site of hCE1 was known to be promiscuous and capable of interacting with a variety of chemically distinct ligands, these structures reveal that the enzyme contains two additional ligand-binding sites and that each site also exhibits relatively non-specific ligand-binding properties. Using this multisite promiscuity, hCE1 appears structurally capable of assembling several catalytic events depending, apparently, on the physiological state of the cellular environment. These results expand our understanding of enzyme promiscuity and indicate that, in the case of hCE1, multiple non-specific sites are employed to perform distinct catalytic actions.

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Nonoxidative Enzymes in the Metabolism of Insecticides

Cited by 57 publications

References 85 publications

Physiological and biochemical effects of botanical extract from Piper nigrum Linn (Piperaceae) against the dengue vector Aedes aegypti Liston (Diptera: Culicidae)

Physiological and biochemical effects of botanical extract from Piper nigrum Linn (Piperaceae) against the dengue vector Aedes aegypti Liston (Diptera: Culicidae)

RNA interference revealed the roles of two carboxylesterase genes in insecticide detoxification in Locusta migratoria

Multisite Promiscuity in the Processing of Endogenous Substrates by Human Carboxylesterase 1

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