certain extent under chemical catalysis, survive. As a result, biocatalytic reactions tend to be "cleaner" and laborious purification of product(s) from impurities emerging through side-reactions can largely be omitted. Regioselectivity and diastereoselectivity: Due to their complex three-dimensional structure, enzymes may distinguish between functional groups which are chemically situated in different regions of the substrate molecule. Enantioselectivity: Since almost all enzymes are made from L-amino acids, enzymes are chiral catalysts. As a consequence, any type of chirality present in the substrate molecule is "recognized" upon the formation of the enzyme-substrate complex. Thus a prochiral substrate may be transformed into an optically active product and both enantiomers of a racemic substrate may react at different rates. These reasons, and especially the latter, are the major reasons why synthetic chemists have become interested in biocatalysis. This interest in turn is mainly due to the need to synthesize enantiopure compounds as chiral building blocks for Pharmaceutical drugs and agrochemicals. Asymmetric biocatalysis The use of biocatalysis to obtain enantiopure compounds can be divided into two different methods: Kinetic resolution of a racemic mixture Biocatalyzed asymmetric synthesis In kinetic resolution of a racemic mixture, the presence of a chiral object (the enzyme) converts one of the stereoisomers of the reactant into its product at a greater reaction rate than for the other reactant stereoisomer. The stereochemical mixture has now been transformed into a mixture of two different compounds, making them separable by normal methodology. Biocatalyzed kinetic resolution is utilized extensively in the purification of racemic mixtures of synthetic amino acids. Many popular amino acid synthesis routes, such as the Strecker Synthesis, result in a mixture of R and S enantiomers. This mixture can be purified by (I) acylating the amine using an anhydride and then (II) selectively deacylating only the L enantiomer using hog kidney acylase. These enzymes are typically extremely selective for one enantiomer leading to very large differences in rate, allowing for selective deacylation. Finally the two products are now separable by classical techniques, such as chromatography. The maximum yield in such kinetic resolutions is 50%, since a yield of more than 50% means that some of wrong isomer also has reacted, giving a lower enantiomeric excess. Such reactions must therefore be terminated before equilibrium is reached. If it is possible to perform such resolutions under conditions where the two substrate- enantiomers are racemizing continuously, all substrate may in theory be converted into enantiopure