Chapter 11. Directed Evolution as a Means to Create Enantioselective Enzymes for Use in Organic Chemistry

  1. Dr. Susanne Brakmann2,
  2. Prof. Dr. Kai Johnsson3
  1. Prof. Dr. Manfred T. Reetz,
  2. Karl-Erich Jaeger

Published Online: 28 MAR 2003

DOI: 10.1002/3527600647.ch11

Directed Molecular Evolution of Proteins: or How to Improve Enzymes for Biocatalysis

Directed Molecular Evolution of Proteins: or How to Improve Enzymes for Biocatalysis

How to Cite

Reetz, M. T. and Jaeger, K.-E. (2003) Directed Evolution as a Means to Create Enantioselective Enzymes for Use in Organic Chemistry, in Directed Molecular Evolution of Proteins: or How to Improve Enzymes for Biocatalysis (eds S. Brakmann and K. Johnsson), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, FRG. doi: 10.1002/3527600647.ch11

Editor Information

  1. 2

    AG “Angewandte Molekulare Evolution”, Institut für Spezielle Zoologie, Universität Leipzig, Talstraße 33, D-04103 Leipzig, Germany

  2. 3

    Insitute of Molecular and Biological Chemistry, Swiss Federal Institute of Technology Lausanne, CH-1015 Lausanne, Switzerland

Author Information

  1. Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45740 Mülheim, Germany

Publication History

  1. Published Online: 28 MAR 2003
  2. Published Print: 22 APR 2002

ISBN Information

Print ISBN: 9783527304233

Online ISBN: 9783527600649

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Keywords:

  • mutagenesis;
  • overexpression;
  • enzymes;
  • high-throughput screening;
  • enantioselectivity;
  • lipases;
  • transaminase;
  • hydantoinase;
  • aldolases

Summary

This chapter contains sections titled:

  • Introduction

  • Mutagenesis Methods

  • Overexpression of Genes and Secretion of Enzymes

  • High-Throughput Screening Systems for Enantioselectivity

  • Examples of Directed Evolution of Enantioselective Enzymes

    • Kinetic resolution of a chiral ester catalyzed by mutant lipases

    • Evolution of a lipase for the stereoselective hydrolysis of a meso-compound

    • Kinetic resolution of a chiral ester catalyzed by a mutant esterase

    • Improving the enantioselectivity of a transaminase

    • Inversion of the enantioselectivity of a hydantoinase

    • Evolving aldolases which accept both D- and L-glyceraldehydes

  • Conclusions