Biochemical and Biophysical Research Communications
Regular ArticleCloning and Sequencing of Rat Liver Carboxylesterase ES-3 (EGASYN)
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Cited by (31)
Esterase 22 and beta-glucuronidase hydrolyze retinoids in mouse liver
2009, Journal of Lipid ResearchCitation Excerpt :In addition to its putative role in retinoid metabolism, two studies suggested that Es3 is involved in the detoxification of xenobiotics. Rat Es3 has been found to hydrolyze acetanilide (35, 36), a compound that exhibits analgesic and antipyretic properties (37). Our studies suggest that murine Es22 is a potent REH compared with the other members of the carboxyl esterase family investigated in this study.
Structure, function and regulation of carboxylesterases
2006, Chemico-Biological InteractionsCitation Excerpt :This was the first report to show that cDNA of liver CarbE has the consensus sequence of the ER retention tetrapeptide (HVEL-COOH). Later, Robbi and Beaufay [35] isolated a cDNA clone of another rat liver pI 5.5 esterase (ES-3, egasyn) that has the consensus sequence of the ER retention tetrapeptide (HTEL-COOH). In a case of mouse liver microsomal CarbE, the carboxyl terminal amino acid sequence of clone Es-N is HTEHK-COOH, which differs from the consensus sequence of the ER retention signal.
Structure, function, and regulation of carboxylesterases
2006, Toxicology of Organophosphate & Carbamate CompoundsStructure, Function, and Regulation of Carboxylesterases
2005, Toxicology of Organophosphate and Carbamate CompoundsAcidic residues emulate a phosphorylation switch to enhance the activity of rat hepatic neutral cytosolic cholesterol esterase
2005, Biochimica et Biophysica Acta - Molecular and Cell Biology of LipidsCitation Excerpt :Although homology modeling placed Ile423 and Met444 in the wall of the substrate binding gorge, Ser506 is distant from the active site, in a surface loop (residues 505–521) at the carboxyl terminal end of an α-helix (α16, residues 484–504) that itself bounds the active site gorge [12]. This helix-loop domain is highly conserved among carboxylesterases [13–32] of many species and in other carboxylic ester hydrolases (EC 3.1.1.X) [33–44], including carboxylester lipase (bile salt-stimulated lipase) [35,38,40,43,44] and cholinesterases [34,36,37,39,41,42]. Others report that this domain mediates the binding of C-reactive protein with rabbit liver carboxylesterases without affecting esterase activity [45].
Effect of flavonoids from various Mediterranean plants on enzymatic activity of intestinal carboxylesterase
2004, BiochimieCitation Excerpt :The GEH and liver CE shared 97% and 98% sequence identity at the amino acid and nucleotide levels, respectively [9]. The pI 5.1 CE isoenzyme was also found in the rat intestinal mucosa [10] and the amino acid sequence of several CE isoenzymes of rat liver are now available [11–15]. The high specificity of intestinal CE towards exogenous ester containing substrate along with the presence of the enzyme in the microsomal and cytosolic fractions [16] suggests that the enzyme may be involved in the cell signal transduction via diacylglycerol and protein kinase [17,18].