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Title: 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
Authors: Botta, Maurizio 
E., Cernia
Corelli, Federico 
Manetti, Fabrizio 
S., Soro
Keywords: C. rugosa; Rh. miehei; 2-Arylpropionic ester; Lipase; Molecular modeling; Non-steroidal antiinflammatory drug precursor; Substrate specificity
Issue Date: 1997
Project: None 
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.
ISSN: 0006-3002
DOI: 10.1016/S0167-4838(96)00181-1
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