title: Purification and characterization of a carboxylesterase from the intestine of the nematode Caenorhabditis elegans.
abstract: The major intestinal esterase from the nematode Caenorhabditis elegans has been purified to essential homogeneity. Starting from whole worms, the overall purification is 9000-fold with a 10% recovery of activity. The esterase is a single polypeptide chain of Mr 60,000 and is stoichiometrically inhibited by organophosphates. Substrate preferences and inhibition patterns classify the enzyme as a carboxylesterase (EC 3.1.1.1), but the physiological function is unknown. The sequence of 13 amino acid residues at the esterase N-terminus has been determined. This partial sequence shows a surprisingly high degree of similarity to the N-terminal sequence of two carboxylesterases recently isolated from Drosophila mojavensis [Pen, J., van Beeumen, J., & Beintema, J. J. (1986) Biochem. J. 238, 691-699].
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002107:Caenorhabditis / Q000201:enzymology*; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004330:Drosophila / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007422:Intestines / Q000201:enzymology*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase