Inhibition or activation of Pseudomonas species lipase by 1,2-ethylene-di- N-alkylcarbamates in detergents

Abstract

1,2-Ethylene-di- N- n-propylcarbamate ( 1) is characterized as an essential activator of Pseudomonas species lipase while 1,2-ethylene-di- N- n-butyl-, t-butyl-, n-heptyl-, and n-octyl-carbamates ( 2–5) are characterized as the pseudo substrate inhibitors of the enzyme in the presence of the detergent taurocholate or triton X-100. The inhibition and activation reactions are more sensitive in taurocholate than in triton X-100. From CD studies, the enzyme changes conformations in the presence of the detergent and further alters conformations by addition of the carbamate activator or inhibitor into the enzyme–detergent adduct. Therefore, this study suggests that the conformational change of lipase during interfacial activation is a continuous process to expose the active site of the enzyme to substrate. From 600 MHz 1H NMR studies, the conformations of the α- and β-methylene moieties of the activator 1,2-ethylene-di- N- n-propylcarbamate in the presence of substrate change after adding taurocholate into the mixture, and the conformations of the β-methylene moieties of the inhibitor 1,2-ethylene-di- N- n-butylcarbamate in the presence of substrate alter after adding taurocholate into the mixture.