These authors contributed equally to this work
α,β-Unsaturated Aldehydes as Substrates for Asymmetric CC Bond Forming Reactions with Thiamin Diphosphate (ThDP)-Dependent Enzymes
Article first published online: 17 MAR 2008
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Advanced Synthesis & Catalysis
Volume 350, Issue 5, pages 759–771, March 25, 2008
How to Cite
Cosp, A., Dresen, C., Pohl, M., Walter, L., Röhr, C. and Müller, M. (2008), α,β-Unsaturated Aldehydes as Substrates for Asymmetric CC Bond Forming Reactions with Thiamin Diphosphate (ThDP)-Dependent Enzymes. Adv. Synth. Catal., 350: 759–771. doi: 10.1002/adsc.200700550
- Issue published online: 18 MAR 2008
- Article first published online: 17 MAR 2008
- Manuscript Received: 21 NOV 2007
- benzaldehyde lyase;
- benzoylformate decarboxylase;
- pyruvate decarboxylase;
The enzymes benzaldehyde lyase (BAL) from Pseudomonas fluorescens, benzoylformate decarboxylase (BFD) from Pseudomonas putida and pyruvate decarboxylase (PDC) from Saccharomyces cerevisiae provide different CC bond forming possibilities of α,β-unsaturated aldehydes with aliphatic and aromatic aldehydes. Structure elucidation and determination of the absolute configuration of the products, which were obtained with high regio- and stereoselectivity were carried out. Selective 1,2-reactivity with yields of 75% and >98% ee, for one single isomer (A) were obtained, by choosing the suitable enzyme in combination with the appropriate substrates. By varying enzymes or substrates the regioisomeric hydroxy ketones C, with up to >99% ee, can be obtained. The application of these new chiral building blocks in the synthesis of natural products or biological active substances is considerably facilitated by applying the different ThDP-dependent enzymes as catalysts.
Abbreviations: BAL, benzaldehyde lyase; BFD, benzoylformate decarboxylase; PDC, pyruvate decarboxylase; His, hexahistidine; 2-HPP, 2-hydroxy-1-phenylpropan-1-one; PAC, phenylacetylcarbinol; NTA, nitrilotriacetic acid; ThDP, thiamin diphosphate; wt, wild-type.