Abstract
Many scientists are trying to create synthetic host molecules which mimic some of the recognition and catalytic properties of real enzymes. Enzymes catalyse chemical reactions with an efficiency that is awe-inspiring: they can bring together two unreactive substrate molecules, induce them to react, and then release the product at an astonishing speed. They are also subtle, usually forming just one of the many products that would result from a simple reaction carried out by a chemist. We know in general terms that enzymes achieve their catalysis by binding two substrate molecules in close proximity, by using binding energy and conformational changes to facilitate the approach to the transition state, and by using their own functional groups to intervene chemically, but we do not know all the rules. In particular we do not understand the balance between structural rigidity leading to pre-organised binding sites, and flexibility which allows the site to recognise and respond to the shape and size of the bound substrate.
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© 1996 Kluwer Academic Publishers
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Walter, C.J., Mackay, L.G., Sanders, J.K.M. (1996). Can Enzyme Mimics Compete with Catalytic Antibodies?. In: Chatgilialoglu, C., Snieckus, V. (eds) Chemical Synthesis. NATO ASI Series, vol 320. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0255-8_18
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DOI: https://doi.org/10.1007/978-94-009-0255-8_18
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