Effect of alcohols on the hydrolysis catalyzed by human pancreatic carboxylic-ester hydrolase
作者： Dominique Lombardo , Odette Guy
DOI: 10.1016/0005-2744(81)90328-4
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摘要: Transfer reactions catalyzed by human pancreatic carboxylic-ester hydrolase (EC 3.1.1.1) were studied in the presence of methanol and butanol as nucleophiles. The addition alcohols produced an increase total rate 4-nitrophenyl acetate n-propylthiol disappearance a concomitant slow decrease hydrolysis rate. These results indicate competitive partitioning acyl-enzyme intermediate between water nucleophile. Moreover, strong inhibition rates methyl butyrate triacetin nucleophiles is agreement with rate-limiting acylation step. kinetic data trans-ester characterization argue favor formation two-step reaction mechanism, deacylation both being rate-limiting. experiments performed show existence nucleophile binding site.
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