@article{discovery10189515, year = {2024}, title = {A transaminase-mediated aldol reaction and applications in cascades to styryl pyridines}, month = {March}, journal = {Catalysis Science \& Technology}, publisher = {Royal Society of Chemistry (RSC)}, note = {{\copyright} The Royal Society of Chemistry 2024. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (http://creativecommons.org/licenses/by/3.0/).}, author = {Hailes, Helen C and Wang, Yu and Li, Yiwen and Ni, Yeke and Bucar, Dejan-Kresimir and Dalby, Paul A and Ward, John M and Jeffries, Jack}, url = {http://dx.doi.org/10.1039/d3cy01370g}, 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.} }