Application of directed evolution in the development of
enantioselective enzymes*
Manfred T. Reetz
Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz
1, D-45470 Mülheim/Ruhr, Germany
Abstract: A novel approach to developing enantioselective enzymes
for use in organic chemistry has been devised which is independent of
structural or mechanistic aspects. The underlying idea is to combine
appropriate methods of random mutagenesis, gene expression, and high-throughput
screening for enantioselectivity. If these actions are performed in
repetitive cycles, an evolutionary pressure is created that leads to
sequential improvements of the enantioselectivity of a given enzyme-catalyzed
reaction. The concept is illustrated by an example involving the lipase-catalyzed
hydrolytic kinetic resolution of an a-chiral
ester, the enantio-selectivity increasing from ee = 2% (E =1.1) for
a wild-type enzyme to ee = 90-93% (E = 25) for the best mutants.
*Lecture presented at the 13th International
Conference on Organic Synthesis (ICOS-13), Warsaw, Poland, 1-5 July
2000.
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