A new generation of smart amine donors for transaminase-mediated biotransformations
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 novel di...
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| Format: | Article |
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Wiley-VCH Verlag
2016
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| Online Access: | https://eprints.nottingham.ac.uk/35260/ |
| _version_ | 1848795038153179136 |
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| author | Gomm, Andrew Lewis, William Green, Anthony P. O'Reilly, Elaine |
| author_facet | Gomm, Andrew Lewis, William Green, Anthony P. O'Reilly, Elaine |
| author_sort | Gomm, Andrew |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | 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 novel 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 via decarboxylation of endogenous lysine. |
| first_indexed | 2025-11-14T19:25:44Z |
| format | Article |
| id | nottingham-35260 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:25:44Z |
| publishDate | 2016 |
| publisher | Wiley-VCH Verlag |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-352602020-05-04T18:01:29Z https://eprints.nottingham.ac.uk/35260/ A new generation of smart amine donors for transaminase-mediated biotransformations Gomm, Andrew Lewis, William Green, Anthony P. O'Reilly, Elaine 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 novel 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 via decarboxylation of endogenous lysine. Wiley-VCH Verlag 2016-07-14 Article PeerReviewed Gomm, Andrew, Lewis, William, Green, Anthony P. and O'Reilly, Elaine (2016) A new generation of smart amine donors for transaminase-mediated biotransformations. Chemistry - a European Journal . ISSN 1521-3765 asymmetric catalysis biocatalysis chiral amine diamine transaminase http://onlinelibrary.wiley.com/doi/10.1002/chem.201603188/abstract doi:10.1002/chem.201603188 doi:10.1002/chem.201603188 |
| spellingShingle | asymmetric catalysis biocatalysis chiral amine diamine transaminase Gomm, Andrew Lewis, William Green, Anthony P. O'Reilly, Elaine A new generation of smart amine donors for transaminase-mediated biotransformations |
| title | A new generation of smart amine donors for transaminase-mediated biotransformations |
| title_full | A new generation of smart amine donors for transaminase-mediated biotransformations |
| title_fullStr | A new generation of smart amine donors for transaminase-mediated biotransformations |
| title_full_unstemmed | A new generation of smart amine donors for transaminase-mediated biotransformations |
| title_short | A new generation of smart amine donors for transaminase-mediated biotransformations |
| title_sort | new generation of smart amine donors for transaminase-mediated biotransformations |
| topic | asymmetric catalysis biocatalysis chiral amine diamine transaminase |
| url | https://eprints.nottingham.ac.uk/35260/ https://eprints.nottingham.ac.uk/35260/ https://eprints.nottingham.ac.uk/35260/ |