Abstract
Transaminase enzymes are well established biocatalysts that are used in chemical synthesis due to their beneficial sustainability profile, regio- and stereoselectivity and substrate specificity. Here, the use of a wild-type Chromobacterium violaceum transaminase (CvTAm) in enzyme cascades revealed the formation of a novel hydroxystyryl pyridine product. Subsequent studies established it was a transaminase mediated reaction where it was exhibiting apparent aldolase reactivity. This promiscuous enzyme reaction mechanism was then explored using other wild-type transaminases and via the formation of CvTAm mutants. Application of one pot multi-step enzyme cascades was subsequently developed to produce a range of hydroxystyryl pyridines.
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