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Esterase

About: Esterase is a research topic. Over the lifetime, 7622 publications have been published within this topic receiving 168270 citations.


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Journal ArticleDOI
TL;DR: Molecular understanding is expanded of the important role of α‐esterases during the development of resistance to organophosphorous insecticides in B. dorsalis and heterologous expression combined with cytotoxicity assay in Sf9 cells demonstrated that BdCarE4 and Bd carE6 can probably detoxify malathion.
Abstract: Esterase has been reported to be involved in malathion resistance in the oriental fruit fly, Bactrocera dorsalis (Hendel) However, the underlying molecular mechanism of the esterase-mediated resistance remains largely unknown in this species Here, with the use of a strain selected for malathion resistance in the laboratory (MR), we found that two overexpressed α-esterase genes, namely BdCarE4 and BdCarE6, predominant in the adult midgut and fat body, function in conferring malathion resistance in B dorsalis Notably, these two genes were found to be mostly close to the esterase E3, which are usually implicated in detoxifying organophosphate insecticides The transcript levels of BdCarE4 and BdCarE6 were investigated and compared between the MR and a susceptible (MS) strain of B dorsalis Both genes were significantly up-regulated in the MR strain, which was consistent with the enhanced esterase activity in the MR strain However, no changes in either the coding sequence or gene copy number were observed between the two strains Subsequently, heterologous expression combined with cytotoxicity assay in Sf9 cells demonstrated that BdCarE4 and BdCarE6 can probably detoxify malathion Furthermore, RNA interference-mediated knockdown of each of these two genes significantly increased malathion susceptibility in the MR strain adults In conclusion, these results expand our molecular understanding of the important role of α-esterases during the development of resistance to organophosphorous insecticides in B dorsalis

59 citations

Journal ArticleDOI
TL;DR: The isolation and purification of a 42.98-kDa latex glycoprotein showing homology to the early nodule-specific protein (ENSP) of the legumes Medicago sativa, Medicago truncatula, and Glycine max is reported, which is allergenic and may be involved in plant defense.

59 citations

Journal ArticleDOI
TL;DR: The gene for proline iminopeptidase from Lactobacillus delbrueckii subsp.
Abstract: The gene for proline iminopeptidase from Lactobacillus delbrueckii subsp. lactis DSM 7290 coding for an enzyme that hydrolyses the synthetic substrate l-prolyl-β-naphthylamide (Pro-βNA) was cloned in Escherichia coli. An enzymic plate assay was used to screen for positive clones. The gene, designated pepl, was subcloned into vector pUC18 and sequenced. The nucleotide sequence revealed an 882 bp open reading frame encoding 294 amino acids, coding for an enzyme with a calculated molecular mass of 32883 Da. By cloning under control of the lac promoter the peptidase was highly expressed. Sequence analysis showed that pepl is of a new sequence type, distinct from all peptidases so far sequenced. Amino acid homology to the active site of a Pseudomonas putida esterase and inhibitor studies of the enzyme imply involvement of a serine residue in catalysis.

59 citations

Journal Article
TL;DR: It was concluded that C′1-esterase is a functional component of complement and that esterolytic activity and C′4 inactivation may be functions of the same catalytic site.
Abstract: Summary Purified C′1-esterase inactivated both C′2 and C′4 in solution. Esterolytic activity and the ability to inactivate C′4 could not be dissociated by inactivation of the enzyme with C′1-esterase inhibitor or DFP, or by denaturation at extremes of temperature or pH. It was concluded that these activities were in all probability properties of the same molecular species. Inhibition of enzymatic activity by DFP blocked both the ability to inactivate C′4 and the ability to bind C′1-esterase inhibitor, suggesting in addition that esterolytic activity and C′4 inactivation may be functions of the same catalytic site Purified C′1-esterase was capable of substituting for C′1s in the formation of EAC′1 with C′1q and C′1r. EAC′1 prepared with C′1-esterase was capable of forming EAC′1,4 with partially purified C′4. It was therefore concluded that C′1-esterase is a functional component of complement.

58 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202391
2022209
202183
2020112
2019107
2018129