Search

The application of ω-transaminase biocatalysts for the synthesis of optically pure chiral amines presents a number of challenges, including difficulties associated with displacing the challenging reaction equilibria. Herein, we report a highly effective approach using low equivalents of the new diamine donor, cadaverine, which enables high conversions of challenging substrates to the corresponding chiral amines in excellent ee. This approach paves the way for the design of self-sufficient fermentation processes combining transaminase biotransformations with existing strategies for cadaverine production by decarboxylation of endogenous lysine. [ABSTRACT FROM AUTHOR]

The "smart" amine donors o‐xylylenediamine and cadaverine were employed for the rapid screening of a large ketone library and subsequent preparative‐scale synthesis of selected compounds using a commercially available amine transaminase, ATA256. The methodology enables both screening and preparative‐scale biotransformations to be performed with a single enzyme and simplifies the generation of sp3‐rich small‐molecule libraries. The "smart" amine donors o‐xylylenediamine and cadaverine have been employed for the rapid screening of a large ketone library and subsequent preparative‐scale synthesis of a selection of optically pure chiral amines, using a commercially available amine transaminase biocatalyst. [ABSTRACT FROM AUTHOR]

The widespread application of ω-transaminases as biocatalysts for chiral amine synthesis has been hampered by fundamental challenges, including unfavorable equilibrium positions and product inhibition. Herein, an efficient process that allows reactions to proceed in high conversion in the absence of by-product removal using only one equivalent of a diamine donor ( ortho-xylylenediamine) is reported. This operationally simple method is compatible with the most widely used ( R)- and ( S)-selective ω-TAs and is particularly suitable for the conversion of substrates with unfavorable equilibrium positions (e.g., 1-indanone). Significantly, spontaneous polymerization of the isoindole by-product generates colored derivatives, providing a high-throughput screening platform to identify desired ω-TA activity. [ABSTRACT FROM AUTHOR]

Herein we report a one-pot protocol for the deracemisation of chiral benzylic amines employing a novel monoamine oxidase-ω-transaminase cascade, allowing access to enantiopure compounds in >99 % ee. We also demonstrate that the same enzymatic cascade can be employed for the dealkylation of secondary amines with >99 % conversion. [ABSTRACT FROM AUTHOR]