Controlling lipase enantioselectivity for organic synthesis.
Lipases are used frequently as chiral catalysts in the synthesis of various fine chemicals and intermediates. The increasing need of compounds with high stereochemical purity requires catalysts with an improved and controlled performance. This overview emphasizes some important aspects for the control of lipase enantioselectivity and some examples where the enantioselectivity has been altered or reversed are highlighted. However, in several of these cases the complete explanation for the altered or reversed enantioselectivity remains unclear and needs to be solved. Three different strategies (engineering of the reaction medium, the substrate molecule, and the enzyme) for exploring lipase enantioselectivity at a molecular level are discussed and summarized. These three different approaches represent powerful tools for understanding the molecular basis for lipase enantioselective catalysis and can guide the rational improvement and tailoring of catalyst performance. By combining approaches from chemistry and biology much is learnt about the most important parameters controlling lipase enantioselectivity for organic synthesis.
Berglund
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Department of Biotechnology, Royal Institute of Technology (KTH), SE-100 44 Stockholm, Sweden. per.berglund@biochem.kth.se
D002625:Chemistry, Organic / Q000379:methods; D019020:Directed Molecular Evolution; D006868:Hydrolysis; D008049:Lipase / Q000235:genetics / Q000378:metabolism*; D008956:Models, Chemical; D008968:Molecular Conformation; D015202:Protein Engineering / Q000379:methods*; D013237:Stereoisomerism; D013379:Substrate Specificity / Q000235:genetics
D008049:Lipase