Journal
ADVANCED SYNTHESIS & CATALYSIS
Volume 350, Issue 5, Pages 759-771Publisher
WILEY-BLACKWELL
DOI: 10.1002/adsc.200700550
Keywords
benzaldehyde lyase; benzoylformate decarboxylase; biocatalysts; pyruvate decarboxylase; stereochemistry
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The enzymes benzaldehyde lyase (BAL) from Pseudomonas fluorescens, benzoylformate decarboxylase (BFD) from Pseudomonas putida and pyruvate decarboxylase (PDC) from Saccharomyces cerevisiae provide different C-C bond forming possibilities of a,p-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.
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