Purification and characterization of a carboxylesterase from the intestine of the nematode Caenorhabditis elegans.
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].
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
D004791:Enzyme Inhibitors; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase