Enantioselectivity of recombinant Rhizomucor miehei lipase in the ring opening of oxazolin-5(4H)-ones

Enantioselectivity of enzyme catalysis is often rationalized via active sit e models. These models are constructed on the basis of comparing the enanti omeric excess of product observed in a series of reactions which are conduc ted with a range of homologous substrates, typically carrying various side chain substitutions. Surprisingly the practical application of these simple but informative 'pocket size' models has been rarely tested in genetic eng ineering experiments. In this paper we report the construction, purificatio n and enantioselectivity of two recombinant Rhizomucor miehei lipases which were designed to check the validity of such a model in reactions of ring o pening of oxazolin-5(4H)-ones.