Steric-control for the enantioselective hydrolysis of amino acid esters with membrane-bound enzyme models

Article abstract of DOI:10.1016/S0040-4039(99)00129-X

The apparently complete stereoselectivity (K(L)(a,obsd)/k(D)(a,obsd)=(∞) for the hydrolysis of enantiomeric substrate (p-nitrophenyl n-dodecanoyl-D(L)-phenyalaninate; C(t2)-D(L)-Phe-PNP) catalyzed by active tripeptide (N-(benzyloxycarbonyl)-L-phenylalanyl-L- histidyl-L-leucine; Z-PheHisLeu) was attained by regulating the composition of coaggregates, ionic strength, and temperature, in coaggregate systems composed of vesicular and micellar surfactants. This can be related to the optimization of conformation in the Z-PheHisLeu catalyst to react with amino acid esters by changing of physical properties of coaggregates.