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& Enzymes Working at the Backbone of Organic Chemistry ''The efficient formation of carbon-carbon bonds forms the backbone of synthetic organic chemistry '' says Barry Trost (Chem Rev 2001, 2067-2096). And biocatalysis nowadays offers some convenient and selective tools for these ''backbone'' transformations. Apart from, for example, aldolases, that have been known for a long time to catalyze enantio-selective C-C bond formations, thiamin diphosphate-dependent enzymes-like pyruvate decarboxylase or benzoylformate decarboxylase-are used for this purpose. This class of enzymes is especially appealing because aromatic and aliphatic aldehydes can be used as substrates, which are more readily available than activated sugars necessary for aldolases. In this work four groups joined forces to apply C-C bond formation catalyzed by thiamin diphosphate-dependent benzaldehyde lyase (BAL) on preparative scale in a continuously operated enzyme membrane reactor. The authors took a truly interdisciplinary approach combining enzymology, bioorganic chemistry, and reaction engineering to obtain different chiral products on gram scale.
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