Selective racemization in preference to transamination catalyzed by pyridoxal enzyme analogs
The racemase activity of pyridoxal enzyme models is selectively increased in preference to transaminase activity by the attachment of rigid basic groups.
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Acknowledgements
This work has been supported by the NIH and the NSF.
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2022, Journal of CatalysisCitation Excerpt :Although the preliminary reaction model has been proposed, the specific role of the side chain substituents on the reaction enantioselectivity remained a challenge. Previous findings have shown that the use of metal salts may be necessary to improve the reactivity and enantioselectivity of chiral pyridoxal analogs-catalyzed asymmetric reactions [15,20]. However, the combination mode between the base and the chiral pyridoxal catalyst and their effect on regulating enantioselectivity need to be clarified.
Ronald C.D. Breslow (1931–2017): A career in review
2021, Bioorganic ChemistryCitation Excerpt :The authors explain that the unusual relationship between pH of solution and chiral preference of the products may be due to catalysis by the protonated form of the transannular, nitrogen-containing chain. Other pyridoxal-catalyzed reactions, including racemization[346] and decarboxylation,[347] have also been reported. Beyond the use of PEIs and PEI derivatives, Breslow and co-workers also investigated polyvinylimidazoles (PVIs) as potential transaminase enzyme mimics.[348]
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