We thank Prof. Dr. G. Höfle from HZI Braunschweig for authentic reference material of aurachin B and C. Y.K. was supported by the Humboldt foundation with a Humboldt Research Fellowship for Postdoctoral Researchers. Research in the laboratory of R.M. was funded by the Deutsche Forschungsgemeinschaft and the Bundesministerium für Bildung und Forschung. FAD=flavin–adenine dinucleotide.
A Semipinacol Rearrangement Directed by an Enzymatic System Featuring Dual-Function FAD-Dependent Monooxygenase†
Article first published online: 21 AUG 2012
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 51, Issue 37, pages 9437–9440, September 10, 2012
How to Cite
Katsuyama, Y., Harmrolfs, K., Pistorius, D., Li, Y. and Müller, R. (2012), A Semipinacol Rearrangement Directed by an Enzymatic System Featuring Dual-Function FAD-Dependent Monooxygenase . Angew. Chem. Int. Ed., 51: 9437–9440. doi: 10.1002/anie.201204138
- Issue published online: 5 SEP 2012
- Article first published online: 21 AUG 2012
- Manuscript Received: 28 MAY 2012
- Humboldt foundation
- Deutsche Forschungsgemeinschaft
- Bundesministerium für Bildung und Forschung
The biosynthesis of aurachins includes the intriguing migration of the prenyl group by a pinacol-type rearrangement. In vitro analysis of AuaGH revealed that these enzymes catalyze epoxidation coupled with semipinacol rearrangement (see scheme) and ketoreduction. Thus, the AuaGH system was revealed to be a novel enzymatic system for establishing semipinacol rearrangements.