Abstract
Over the last several years we have been witnessing the proliferation of enzymatic synthetic methods in organic chemistry. More and more organic chemists without any special training in enzymology use enzymes as catalysts on a routine basis. Enzymes have a number of properties useful in organic synthesis, but their greatest advantage over standard chemical techniques is selectivity. Different levels of enzyme selectivity — substrate specificity, regio-, chemo- or stereoselectivity — may be successfully exploited in the synthesis of complex, polyfunctional molecules. The optimal situation would be to have a catalyst which can accomodate as many subtrates as possible (broad substrate specificity) and then carry out the catalytic transformation in a selective way. The recent discovery that substrate specificity and enantioselectivity of enzymes may be dramatically altered, and sometimes predictably controlled by changing the reaction medium creates new opportunities for organic chemistry.1–5
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Margolin, A.L. (1990). Exploiting Enzyme Selectivity for the Synthesis of Biologically Active Compounds. In: Baldwin, T.O., Raushel, F.M., Scott, A.I. (eds) Chemical Aspects of Enzyme Biotechnology. Industry-University Cooperative Chemistry Program Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9637-7_16
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DOI: https://doi.org/10.1007/978-1-4757-9637-7_16
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