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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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TL;DR: No lactonase activity was found in homogenates of rat brain, spleen, kidney, heart, and diaphragm, although rat serum and plasma do contain the enzyme, and the γ-lactonase enzymes also catalyze lactonization of the corresponding γhydroxy acids.
94 citations
TL;DR: A spectrophotometric assay for the quantitative determination of feruloyl esterase activity based on release of 4-nitrophenol from a novel substrate, 4-Nitrophenyl ferulate in an emulsion of Triton X-100 in aqueous buffer solution is developed.
94 citations
TL;DR: The results suggest that the AtGELP genes have diverse physical functions such as affecting the germination rate and early growth of seedlings subjected to high concentrations of glucose, or being involved in biotic stress responses.
Abstract: In this present study, we introduce a fundamental framework and provide information regarding the possible roles of GDSL-type esterase/lipase gene family in Arabidopsis. GDSL-type esterases/lipases are hydrolytic enzymes with multifunctional properties such as broad substrate specificity, regiospecificity, and stereoselectivity. In this study, we identified 105 GDSL-type esterase/lipase genes in Arabidopsis thaliana by conducting a comprehensive computational analysis. Expression studies indicated that GDSL-type lipase proteins showed varied expression patterns. Phylogenetic tree analysis indicated that AtGELP (Arabidopsis thaliana GDSL-type esterase/lipase protein) gene family was divided into four clades. The phylogenetic analysis, combined with protein motif architectures, and expression profiling were used to predict the roles AtGELP genes. To investigate the physical roles of the AtGELP gene family, we successfully screened 88 AtGELP T-DNA knockout lines for 54 AtGELP genes from 199 putative SALK T-DNA mutants. Transgenic plants of AtGELP genes were used to elucidate the phenotypic characteristics in various developmental stages or stress conditions. Our results suggest that the AtGELP genes have diverse physical functions such as affecting the germination rate and early growth of seedlings subjected to high concentrations of glucose, or being involved in biotic stress responses.
94 citations
TL;DR: Although 2,3,7,8-tetrachlorodibenzo-p-dioxin treatment induces this esterase severalfold, the amino acid sequence of the induced enzyme is identical to that of the enzyme isolated from liver microsomes of untreated rabbits.
94 citations
TL;DR: Evidence for the identity of the two enzymes, carboxylesterase and aryl acylamidase, was their co-elution profiles and co-purification in the different steps, including electrophoresis, with constant ratios of specific activities and percentage recoveries.
Abstract: The three enzyme activities, carboxylesterase, aryl acylamidase and cholinesterase activities, have been found in rat and human sera. Rat serum carboxylesterase associated with serum aryl acylamidase activity, but not with serum cholinesterase activity, was purified by ammonium sulfate precipitation, followed by successive chromatographies on DEAE-cellulose, blue Sepharose and QAE-Sephadex, and then electrophoresis. Evidence for the identity of the two enzymes, carboxylesterase and aryl acylamidase, was their co-elution profiles and co-purification in the different steps, including electrophoresis, with constant ratios of specific activities and percentage recoveries. Human serum carboxylesterase associated with serum cholinesterase, purified earlier, was compared with the rat serum esterase. Human serum carboxylesterase and aryl acylamidase activities were inhibited by serotonin and neostigmine, whereas rat serum carboxylesterase and aryl acylamidase activities were not affected by these compounds. Tyramine activated human but not rat aryl acylamidase. Rat and human serum esterase activities were both strongly inhibited by the diisopropylfluorophosphate. Both esterases catalyzed the hydrolysis of short-chain triacylglycerols, such as tributyrin, and medium-chain monoacylglycerols, such as monocaprin, but not the hydrolysis of long-chain triacylglycerols.
93 citations