The classification of esterases: an important gene family involved in insecticide resistance - A review

Montella, Isabela Reis; Schama, Renata; Valle, Denise

doi:10.1590/s0074-02762012000400001

Cited by 198 publications

(166 citation statements)

References 92 publications

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“…These crystals all belonged to the same space group P3 2 21 and diffracted beyond a resolution of 1.2 A. They were subsequently soaked with different ligands at both physiological and low pH.…”

Section: Structure Of Ttestmentioning

confidence: 99%

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Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis

et al. 2015

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Thermogutta terrifontis esterase (TtEst), a carboxyl esterase identified in the novel thermophilic bacterium T. terrifontis from the phylum Planctomycetes, has been cloned and over-expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity towards small p-nitrophenyl (pNP) carboxylic esters, with optimal activity for pNPpropionate. The enzyme retained 95% activity after incubation for 1 h at 80°C. The crystal structures of the native TtEst and its complexes with the substrate analogue D-malate and the product acetate have been determined to high resolution. The bound ligands have allowed the identification of the carboxyl and alcohol binding pockets in the enzyme active site. Comparison of TtEst with structurally related enzymes provides insight into how differences in their catalytic activity can be rationalized based upon the properties of the amino acid residues in their active site pockets. The mutant enzymes L37A and L251A have been constructed to extend the substrate range of TtEst towards the larger butyrate and valerate pNPesters. These mutant enzymes have also shown a significant increase in activity towards acetate and propionate pNP esters. A crystal structure of the L37A mutant was determined with the butyrate product bound in the carboxyl pocket of the active site. The mutant structure shows an expansion of the pocket that binds the substrate carboxyl group, which is consistent with the observed increase in activity towards pNP-butyrate.

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Section: Structure Of Ttestmentioning

confidence: 99%

“…They are widely distributed in bacteria, archaea and eukaryotes [2]. They have been used extensively in industry as a result of their versatility, robustness and stereoselectivity, as well as their ability to promote synthetic reactions in organic solvents in the absence of water [3].…”

Section: Introductionmentioning

confidence: 99%

Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis

et al. 2015

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“…As is well known in pharmaceuticals, knowledge of the key interactions between a drug and the organisms it acts upon can enable drug discovery and assist in effective resistance management. Metabolism of pesticides in insects has an important effect on drug potency and plays a key role in insecticide resistance in a number of cases [19][20][21][22]. Research using C. elegans as a model organism has facilitated the identification of the protein target of the BZs.…”

Section: Introductionmentioning

confidence: 99%

NHR-176 regulates cyp-35d1 to control hydroxylation-dependent metabolism of thiabendazole in Caenorhabditis elegans

Jones

Flemming

Urwin

2015

Biochemical Journal

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Knowledge of how drugs are metabolized and excreted is an essential component of understanding their fate within and among target and non-target organisms. Thiabendazole (TBZ) was the first benzimidazole (BZ) to be commercially available and remains one of the most important anthelmintic drugs for medical and veterinary use. We have characterized how Caenorhabditis elegans metabolizes and excretes TBZ. We have shown that TBZ directly binds to the nuclear hormone receptor (NHR)-176 and that this receptor is required for the induction by TBZ of the cytochrome P450 (CYP) encoded by cyp-35d1. Further, RNAi inhibition of cyp-35d1 in animals exposed to TBZ causes a reduction in the quantity of a hydroxylated TBZ metabolite and its glucose conjugate that is detected in C. elegans tissue by HPLC. This final metabolite is unique to nematodes and we also identify two P-glycoproteins (PGPs) necessary for its excretion. Finally, we have shown that inhibiting the metabolism we describe increases the susceptibility of C. elegans to TBZ in wild-type and in resistant genetic backgrounds.

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“…3-5 suggest that ester-hydrolyzing enzymes, specifically esterases and lipases secreted by B. cereus are responsible for the structural and luminescent transformations observed in the C-dot-hydrogel system. 40,41 Esterases constitute a diverse enzyme family secreted by both mammalian and bacterial cells, which function through hydrolysis of ester bonds in target substrates. 42 Notably, the hydrogel scaffold contains a multitude of ester bonds, both positioned in polar environments (e.g.…”

Section: 35mentioning

confidence: 99%

Carbon-dot–hydrogel for enzyme-mediated bacterial detection

2017

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A hybrid carbon-dot (C-dot)-hydrogel matrix was constructed and employed for detection of bacteria. The transduction mechanism is novel, based upon cleavage of ester bonds within the hydrogel scaffold by bacterially-secreted esterases; the ensuing fluidization of the hydrogel resulted in aggregation of the embedded C-dots and consequent quenching of their fluorescence. We show that the C-dot-hydrogel exhibits high sensitivity and can distinguish among bacterial species through modulation of the emitted fluorescence, depending upon their esterase secretions.

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The classification of esterases: an important gene family involved in insecticide resistance - A review

Cited by 198 publications

References 92 publications

Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis

Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis

NHR-176 regulates cyp-35d1 to control hydroxylation-dependent metabolism of thiabendazole in Caenorhabditis elegans

Carbon-dot–hydrogel for enzyme-mediated bacterial detection

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