From Commercial Enzymes to Biocatalysts Designed by Protein Engineering

Uwe T. Bornscheuer

doi:10.1055/s-0032-1317498

Synlett, Table of Contents

Synlett 2013; 24(2): 150-156
DOI: 10.1055/s-0032-1317498

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From Commercial Enzymes to Biocatalysts Designed by Protein Engineering

Uwe T. Bornscheuer*

Department of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany Fax: +49(3834)86794367 Email: uwe.bornscheuer@uni-greifswald.de

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Abstract

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Abstract

This account provides a personal view on the development of biocatalysis over the last two decades. Examples include the use of commercial enzymes, such as lipases, (recombinant) esterases, transaminases, and Baeyer–Villiger monooxygenases for the synthesis of optically pure compounds. The opportunity provided by modern protein engineering methods to tailor design an enzyme for a given scientific problem (substrate scope, selectivity, stability) is emphasized together with concepts to boost this technology in terms of timelines and success.

1 Introduction

2 Unexpected Discoveries

2.1 To Protect and Serve

2.2 ‘Abnormal’ Access to β-Amino Acids

3 Defined Enzyme Is Better Than Crude Extract

4 New Horizons Opened by Protein Engineering

4.1 Random Mutagenesis Can Give Random Results

5 Exploring Sequence and Structure Databases

5.1 Massive Alignment Identifies Evolutionary Variations

5.2 Fixing Wrong Annotations Can Yield a Toolbox of Novel Enzymes

6 Conclusion

Key words

asymmetric catalysis - biocatalysis - enantioselectivity - enzymes - kinetic resolution - protein engineering

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References

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