Communication

Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes†

  1. Stefan Becker Dr.1,
  2. Horst Höbenreich2,
  3. Andreas Vogel Dr.2,
  4. Janina Knorr3,
  5. Susanne Wilhelm Dr.3,
  6. Frank Rosenau Dr.3,
  7. Karl-Erich Jaeger Prof. Dr.3,
  8. Manfred T. Reetz Prof. Dr.2,
  9. Harald Kolmar Prof. Dr.1

Article first published online: 2 JUN 2008

DOI: 10.1002/anie.200705236

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 47, Issue 27, pages 5085–5088, June 23, 2008

Additional Information

How to Cite

Becker, S., Höbenreich, H., Vogel, A., Knorr, J., Wilhelm, S., Rosenau, F., Jaeger, K.-E., Reetz, Manfred T. and Kolmar, H. (2008), Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes. Angew. Chem. Int. Ed., 47: 5085–5088. doi: 10.1002/anie.200705236

Author Information

  1. 1

    Institute for Biochemistry and Organic Chemistry, Technische Universität Darmstadt, Petersenstrasse 22, 64287 Darmstadt (Germany), Fax: (+49) 6151-16-5399 http://www.biochemie-tud.de

  2. 2

    Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim/Ruhr (Germany)

  3. 3

    Institute of Molecular Enzyme Technology, Heinrich-Heine-Universität Düsseldorf, Research Centre Jülich, 52426 Jülich (Germany)

  1. †

    We thank Deutsche Forschungsgemeinschaft for funding through SPP 1170.

Publication History

  1. Issue published online: 16 JUN 2008
  2. Article first published online: 2 JUN 2008
  3. Manuscript Revised: 7 FEB 2008
  4. Manuscript Received: 14 NOV 2007

Funded by

  • Deutsche Forschungsgemeinschaft. Grant Number: SPP 1170

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Keywords:

  • asymmetric catalysis;
  • directed evolution;
  • enzyme catalysis;
  • hydrolases;
  • kinetic resolution
Thumbnail image of graphical abstract

Getting a look in: A high-throughput screening method has been developed for the identification and isolation of enantioselective hydrolases displayed on cell surfaces (see scheme; E: Esterase, P: Peroxidase). Enantiomeric substrates labeled with two different fluorescent dyes allow real-time analysis of enantioselectivity by determination of the ratio of green and red single-cell fluorescence.

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