Probing the substrate specificity for lipases. A CoMFA approach for predicting the hydrolysis rates of 2-arylpropionic esters catalyzed by Candida rugosa lipase
| Autor: | Fabrizio Manetti, Maurizio Botta, Simonetta Soro, Enrico Cernia, Federico Corelli |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular C. rugosa Biophysics Biochemistry Substrate Specificity Catalysis Reaction rate Hydrolysis Structural Biology Enzymatic hydrolysis Organic chemistry Substrate specificty Lipase Molecular Biology 2-Arylpropionic ester Comparative molecular field analysis Candida chemistry.chemical_classification Phenylpropionates biology Substrate (chemistry) Candida rugosa Enzyme Models Chemical chemistry biology.protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1296:121-126 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(96)00064-7 |
| Popis: | The enzyme catalyzed hydrolysis of esters 1–3, precursors of therapeutically important non-steroidal antiinflammatory drugs, in the presence of the lipase from Candida rugosa was studied and the relative rates of the enzymatic hydrolysis were determined. With the exception of 3, which was not transformed under the reaction conditions, all transformations proved to be highly enantiospecific. Usually the mechanism of enantiorecognition is probed by substrate mapping. Although more theoretical approaches are existing, these all require knowledge of the three-dimensional structure of the enzyme. A model capable of correlating the extent of substrate hydrolysis as well as the initial reaction rates with their stereoelectronic properties has been developed by a Comparative Molecular Field Analysis (CoMFA) approach. This model does not require detailed knowledge of the three-dimensional structure of the enzyme and proved to be highly predictive. It is possible that this kind of approach holds promise for future work on enzyme-substrate interactions. |
| Databáze: | OpenAIRE |
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