The aims of this module are

• To introduce students to the main classes of organic reactions that can be catalysed by enzymes for organic synthesis
• To create an appreciation of the application of biocatalysts in industry
• To introduce strategies for improving biocatalysts by directed evolutior

By the end of the module, students should:

• Understand how enzymes can be applied in organic synthesis
• Have an awareness of current limitations in the application of biocatalysts
• Demonstrate a knowledge of key classes of enzyme reactions.
• Show an understanding of cofactor requirements and recycling strategies
• Have an appreciation of the use directed evolution methods for enzyme improvement

Enzymes are widely used as catalysts for the synthesis of pharmaceuticals, speciality and industrial chemicals. For example, naturally occuring penicillins are modified using enzymes to make semi-synthetic versions that are less prone to antibiotic resistant strains. Many chiral products are made in high enantiomeric purity using enzymes to catalyse enantioselective reactions. Polyacrylamide is made on a very large scale using acrylamide that is made by enzymatic hydrolysis of acrylonitrile. In this module students will be introduced the main classes of enzymes used in biocatalysis and discover how they can be applied in the short and efficient (chemoenzymatic) synthesis of a range of high value materials. Particular emphasis will be placed on application in the synthesis of pharmaceuticals and agrochemicals. Current and future challenges for the area of biocatalysis will be discussed, such as the use of directed evolution to c reate "designer enzymes" with improved attributes such as stability, activity and enantioselectivity.

• Introduction to enzymes – structure and function
• Organic reaction types which can be carried out using enzymes
• Chiral selectivity: kinetic resolution of enantiomers, desymmetrisation of prochiral and meso compounds
• Large scale commercial applications – an introduction.
• Hydrolytic reactions: lipases, esterases, proteases including catalytic triad mechanism. Nitrile hydratases, epoxide hydrolases. 
• Reactions in organic solvents: using lipases and proteases in reverse - applications in industry
• Immobilisation techniques: use of polymer supports and absorption methods.
• Reduction reactions: asymmetric reduction of ketones and ketoesters, nitro group reduction, reduction of C=C bonds, recycling of cofactors.
• Oxidation reactions: hydroxylation, asymmetric sulphoxidation and epoxidation, Baeyer Villiger rearrangement, asymmetric dihydroxylation of aromatics – application in the synthesis of natural products.
• Carbon-carbon bond forming reactions:  asymmetric aldol reaction, acyl group transfer, cyanohydrin formation.
• Directed evolution of enzymes – mutation techniques and screening/selection strategies. Future prospects.

The course will be delivered through a series of 50 minute lectures (16) and two 1 hour tutorials.

Biotransformations for Organic Chemistry – a Textbook, 5^th Ed., Kurt Fabe Publisher:Springer-Verlag Berlin and Heidelberg GmbH & Co. K ISBN: 3540200975