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- W1562273765 abstract "Publisher Summary This chapter summarizes the various classes of cholesterol esterase (CEase) inhibitors and describes the methods for characterizing inhibition by carbamates. It outlines features of CEase structure and function that facilitate the rational design of inhibitors. Physiological lipid substrates of CEase have very low water solubilities, and consequently are contained in supramolecular aggregates, such as micelles or lipoproteins. Accordingly, physiological CEase catalysis is interfacial biocatalysis, wherein substrate binding to the active site and consequent catalytic turnover are preceded by reversible binding of the enzyme to the lipid/aqueous interface. The mechanistic complexity of interfacial biocatalysis makes characterization of the inhibition mechanisms of CEase inhibitors a nontrivial task. Although it is the only pancreatic enzyme with high hydrolytic activity for cholesteryl esters, CEase nonetheless catalyzes hydrolytic and synthetic reactions of a wide range of substrates." @default.
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- W1562273765 date "1997-01-01" @default.
- W1562273765 modified "2023-09-23" @default.
- W1562273765 title "[11] Mechanism-based inhibitors of mammalian cholesterol esterase" @default.
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- W1562273765 doi "https://doi.org/10.1016/s0076-6879(97)86013-2" @default.
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