Effect of sulfonates on the esterase activity of carboxypeptidase A.
The effects of sulfonates on the carboxypeptidase A catalyzed hydrolysis of the ester substrate benzoylglycyl-L-phenyllactate were determined. The modifiers examined were benzenesulfonate, p-toluenesulfonate, 2-phenylethane-sulfonate, methanesulfonate, ethanesulfonate, propanesulfonate, butanesulfonate, pentanesulfonate, hexanesulfonate, heptanesulfonate, and 2,2-dimethyl-2-silapentane-5-sulfonate. Sulfonate activators of peptide hydrolysis were inhibitors of esterase activity. Of the sulfonates studied, 2,2-dimethyl-2-silapentane-5-sulfonate was the most effective inhibitor. 2-Phenylethanesulfonate, hexanesulfonate, heptanesulfonate, and 2,2-dimethyl-2-silapentane-5-sulfonate exhibited uncompetitive inhibition. The remaining sulfonates either did not inhibit or the inhibition was too weak to properly characterize.
Frye
J L
JL
Department of Chemistry, Miami University, Oxford, OH 45056.
Sebastian
J F
JF
D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D043422:Carboxypeptidases A; D004950:Esterases / Q000037:antagonists & inhibitors*; D006626:Hippurates / Q000378:metabolism; D007700:Kinetics; D007773:Lactates / Q000378:metabolism; D013451:Sulfonic Acids / Q000494:pharmacology*
D006626:Hippurates; D007773:Lactates; D013451:Sulfonic Acids; C066372:benzoylglycyl phenyllactate; D004950:Esterases; D002268:Carboxypeptidases; D043422:Carboxypeptidases A