Transaminases are pyridoxal 5'-phosphate (PLP)-dependent enzymes that catalyze the reversible transfer of an amine from a donor substrate to a ketone or aldehyde via a ping-pong mechanism. The synthetic value of transaminases is derived from their ability to furnish enantioenriched primary amines, and this transmission of chiral information from catalyst to product has been extended to adjacent stereocenters via dynamic kinetic resolutions (DKRs, Scheme 1A). Because transaminase-catalyzed reactions are reversible, several strategies to drive equilibria toward the product have been explored. One approach is to load a vast excess of amine donor, such as isopropylamine (IPAm), but this often requires protein engineering to bolster the enzyme's tolerance to the donor or its resultant ketone. Another approach is to dynamically remove the donor byproduct by either evaporation or enzymatic degradation, but these strategies increase the operational complexity. A third approach, and a promising alternative to the former two, is to deploy "smart" amine donors that, upon transamination, undergo further thermodynamically favored cyclization reactions (Scheme 1B). Two prominent examples are cadaverine, whose byproduct undergoes cyclization and then trimerization, and ortho-xylenediamine, which forms isoindoles that further polymerize. While others have also been described, each suffers from one or more of the following drawbacks: high cost, complications to product isolation, and low transaminase compatibility. Consequently, the identification of a smart donor that bypasses these obstacles would be of great value.