Stereoselective inhibition of cholesterol esterase by enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates.

Protein J.2011 Mar;30(3):220-7. doi:10.1007/s10930-011-9323-3

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Four stereoisomers of 2-norbornyl-N-n-butylcarbamates are characterized as the pseudo substrate inhibitors of cholesterol esterase. Cholesterol esterase shows enantioselective inhibition for enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates. For the inhibitions by (R)-(+)- and (S)-(-)-exo-2-norbornyl-N-n-butylcarbamates, the R-enantiomer is 6.8 times more potent than the S-enantiomer. For the inhibitions by (R)-(+)- and (S)-(-)-endo-2-norbornyl-N-n-butyl-carbamates, the S-enantiomer is 4.6 times more potent than the R-enantiomer. The enzyme-inhibitor complex models have been proposed to explain these different enantioselectivities.

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Stereoselective inhibition of cholesterol esterase by enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates.

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