Binding site of acyl moiety in ester hydrolysis by Candida rugosa lipase

The sizes of the large, medium, and small substituent recognition sites (L, M, and S pockets, respectively) in Candida rugosa lipase (CRL) were roughl y estimated by measuring the specific hydrolytic activity against several p -nitrophenyl esters. These relative sizes were assessed as L pocket > pheny l, ethyl > M pocket > methyl > S pocket > hydrogen. The hydrolysis of a ser ies of p-nitrophenyl esters of omega -substituted fatty acids was also exam ined. In this series, p-nitrophenyl esters having one methylene between the ester-carbonyl carbon and cyclohexyl, phenyl, or isopropyl moiety largely demonstrated decreases in hydrolytic activity. (C) 2001 Elsevier Science B. V. All rights reserved.