A.T. and H.H. have contributed equally. We thank R. Sterner (Universität Regensburg) for providing the plasmids for tHisF and mutant Cys9Ala/Asp11Cys, N. Dickmann (Max-Planck-Institut für Bioanorganische Chemie) for MALDI-TOF measurements and M. Rusek for performing some of the fermentations. This work was supported by the Fonds der Chemischen Industrie, the Deutsche Forschungsgemeinschaft (SPP 1170, Re 359/13-1), and the EU (IBAAC MCRTN-CT-2003-505020).
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Communication
Alternate-Site Enzyme Promiscuity†
Article first published online: 2 OCT 2007
DOI: 10.1002/anie.200702751
Copyright © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
Angewandte Chemie International Edition
Volume 46, Issue 45, pages 8597–8600, November 19, 2007
Additional Information
How to Cite
Taglieber, A., Höbenreich, H., Carballeira, J. Daniel., Mondière, Régis J. G. and Reetz, Manfred T. (2007), Alternate-Site Enzyme Promiscuity. Angew. Chem. Int. Ed., 46: 8597–8600. doi: 10.1002/anie.200702751
- †
Publication History
- Issue published online: 8 NOV 2007
- Article first published online: 2 OCT 2007
- Manuscript Revised: 30 AUG 2007
- Manuscript Received: 22 JUN 2007
Funded by
- Fonds der Chemischen Industrie
- Deutsche Forschungsgemeinschaft. Grant Number: Re 359/13-1
- EU. Grant Number: IBAAC MCRTN-CT-2003-505020
Keywords:
- bioconjugation;
- enzyme catalysis;
- enzyme promiscuity;
- hydrolases;
- kinetic resolution
Promiscuous reactions get around: It is shown that promiscuous enzyme-catalyzed reactions (i.e., the catalysis of distinctly different chemical transformations) can also take place at sites other than where the natural reaction occurs.