Exploring the synthetic potential of a marine transaminase including discrimination at a remote stereocentre.
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Date
2020-10-23
Authors
Schwarz, Maria
Murphy, Edel J.
Foley, Aoife M.
Woods, David F.
Castilla, Ignacio Abreu
Reen, F. Jerry
Collins, Stuart G.
O'Gara, Fergal
Maguire, Anita R.
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Journal ISSN
Volume Title
Publisher
Royal Society of Chemistry
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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.
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Keywords
Marine microorganism , Biotechnology , Medical therapeutics , Marine transaminase
Citation
Schwarz, M., Murphy, E. J., Foley, A. M., Woods, D. F., Castilla, I. A., Reen, F. J., Collins, S. G., O'Gara, F. and Maguire, A. R. (2021) 'Exploring the synthetic potential of a marine transaminase including discrimination at a remote stereocentre', Organic & Biomolecular Chemistry, 19(1), pp. 188-198. doi: 10.1039/d0ob01848a
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© The Royal Society of Chemistry 2021