Studies on the enzymatic synthesis of optically pure tertiary alcohols

This books deals with a catalytic platform for the enzymatic synthesis of tertiary alcohols. A certain class of hydrolases bearing the GGG(A)X-motif are efficient and highly selective catalysts for this difficult reaction. The number of available biocatalysts could be extended by making use of a structure-guided screening in metagenome-derived enzyme libraries. Two highly selective enzymes were identified. One model enzyme, esterase BS2, was optimized and the hydrolysis of tertiary esters was studied in detail. In a protein design study, novel enzyme variants were generated by semi-rational protein design methods, which led to the identification of mutants with strongly increased or even inverse enantioselectivity. The application of the platform to the kinetic resolution of a building block of pharmaceutical interest is described.

Autorentext

Robert Kourist, PhD: PostDoc at Keio University, Yokohama, Japan. Research stays in Stockholm, Sweden and Oviedo, Spain. Obtained his PhD degree in Biotechnology under the supervision of Prof. Uwe T. Bornscheuer at the University of Greifswald. His research deals with biocatalysis and the creation of highly selective enzymes by protein design.