Racemic arylpropionic esters 1-3, precursors of therapeutically important non-steroidal antiinflammatory drugs, were subjected to hydrolyses in the presence of either Candida rugosa or Rhizomucor miehei crude lipases. The hydrolyses of 1 and 2 proved to be highly enantioselective, whereas 3 was not transformed at all. Both the substrate specificity and the enantioselectivity of these lipases were explained through a molecular modeling study involving docking experiments between 1-3 and the amino acids forming the enzymes active-sites, whose three-dimensional structures were obtained from X-ray crystallographic data, followed by extensive conformational analysis on their computer-generated complexes. The results of this study also account for the high enantioselective and good yielding hydrolysis of 3 (as the corresponding 2-chloroethyl ester) catalyzed by CRL pretreated with 2-propanol, recently reported in the literature, and lead to admit that such a treatment may operate very deep conformational changes on the amino acids of the enzyme active-site.
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|Titolo:||Probing the substrate specificity for lipases. II. Kinetic and Modeling Studies on the Molecular Recognition of 2-Arylpropionic Esters by Candida rugosa and Rhizomucor miehei Lipases|
|Rivista:||BIOCHIMICA ET BIOPHYSICA ACTA|
|Citazione:||Botta, M., E., C., Corelli, F., Manetti, F., & S., S. (1997). Probing the substrate specificity for lipases. II. Kinetic and Modeling Studies on the Molecular Recognition of 2-Arylpropionic Esters by Candida rugosa and Rhizomucor miehei Lipases. BIOCHIMICA ET BIOPHYSICA ACTA, 1337(2), 302-310.|
|Appare nelle tipologie:||1.1 Articolo in rivista|