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Title: Molecular basis for the stereospecificity of Candida rugosa lipase (CRL) towards ibuprofen
Authors: Lakshmi, B.S.
Kangueane, P.
Guo, Y.
Chen, Y.Z. 
Gautam, P.
Keywords: Candida rugosa lipase
Molecular modelling
Issue Date: 2000
Source: Lakshmi, B.S.,Kangueane, P.,Guo, Y.,Chen, Y.Z.,Gautam, P. (2000). Molecular basis for the stereospecificity of Candida rugosa lipase (CRL) towards ibuprofen. Biocatalysis and Biotransformation 17 (6) : 475-486. ScholarBank@NUS Repository.
Abstract: The stereospecific esterification of ibuprofen by Candida rugosa lipase (CRL) with 1-butanol was optimised. The yield of the butyl ester was nearly quantitative with an enantiomeric excess of 95% and E > 100. Enzyme desiccation over P2O5 had a pronounced effect on the esterification yield and its role in stereospecificity is discussed. Molecular modelling and energy-minimisation studies were also performed to understand the stereospecific binding of substrates to the active site of CRL. The docking of the substrate S(+) ibuprofen to the active site of CRL was performed based on the three-dimensional structure of CRL (PDB entry 1CRL). The results show that only the active S(+) enantiomer of ibuprofen is able to form direct contacts with the reactive hydroxyl group (Ser209) and imidazole base (His449) at the active site, whereas with the R enantiomer the functional group COOH points away from the (His449) base of CRL. This is in accordance with experimental results which shows that the stereospecificity of CRL is towards S(+) ibuprofen.
Source Title: Biocatalysis and Biotransformation
ISSN: 10242422
Appears in Collections:Staff Publications

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