Exploring the synthetic potential of a marine transaminase including discrimination at a remote stereocentre?

Organic & Biomolecular Chemistry Pub Date: 2020-10-23 DOI: 10.1039/D0OB01848A

Abstract

The marine transaminase, P-ω-TA, can be employed for the transamination from 1-aminotetralins and 1-aminoindanes with differentiation of stereochemistry at both the site of reaction and at a remote stereocentre resulting in formation of ketone products with up to 93% ee. While 4-substituents are tolerated on the tetralin core, the presence of 3- or 8-substituents is not tolerated by the transaminase. In general P-ω-TA shows capacity for remote diastereoselectivity, although both the stereoselectivity and efficiency are dependent on the specific substrate structure. Optimum efficiency and selectivity are seen with 4-haloaryl-1-aminotetralins and 3-haloaryl-1-aminoindanes, which may be associated with the marine origin of this enzyme.

Graphical abstract: Exploring the synthetic potential of a marine transaminase including discrimination at a remote stereocentre
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