Topic
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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TL;DR: Results show that use of a specific assay and the demonstration of degradation of malathion in vivo are essential for assessment of the contribution of esterase activity to the malathions-resistant phenotype in mosquito populations.
50 citations
TL;DR: In the fourth stadium in Culex quinquefasciatus as mentioned in this paper, JH epoxide hydrolase activity peaked in 36-h-old fourth instars and pharate pupae at levels 5.7 and 3.0 times that of JH esterase, respectively.
50 citations
TL;DR: Kinetic studies with various substrates show that the enzyme is specific for sialic acids and selectively cleaves acetyl groups in the 9-position, and shows little activity against a variety of other natural compounds bearing O-acetyl esters.
50 citations
TL;DR: This article corrects the article on p. 3208 in vol.
Abstract: The gene coding for a novel esterase which stereoselectively hydrolyzes the (+)-trans (1R,3R) stereoisomer of ethyl chrysanthemate was cloned from Arthrobacter globiformis SC-6-98-28 and overexpressed in Escherichia coli. The cellular content of the active enzyme reached 33% of the total soluble protein in the recombinant E. coli JM105 cells and 5.6 g/liter of culture by high-density cell cultivation. The hydrolytic activity of the recombinant E. coli cells for ethyl chrysanthemate reached 605 mumol of chrysanthemic acid per min per g of dry cells, which is approximately 2,500-fold higher than that of A. globiformis cells. The stereoselective hydrolysis by the recombinant E. coli cells was efficient at substrate concentrations of up to 40% by removing the produced chrysanthemic acid by ultrafiltration. The (+)-trans-chrysanthemic acid produced had 100% optical purity. The amino acid sequence of the esterase was found to be similar to that of several class C beta-lactamases, D,D-carboxypeptidase, D-aminopeptidase, 6-aminohexanoate-dimer hydrolase, and Pseudomonas esterase. The sequence comparison also suggested that the Ser-X-X-Lys motif in the esterase was at the active site of the enzyme.
50 citations
TL;DR: In this paper, the salivary esterase activity was identified in the degradation of Bisphenol A-glycidylmethacrylate (BisGMA) and TEGDMA.
50 citations