Keenan, Tessa, Parmeggiani, Fabio, Malassis, Julien et al. (13 more authors) (2020) Profiling substrate promiscuity of wild-type sugar kinases for multifluorinated monosaccharides. Cell Chemical Biology. ISSN 2451-9448
Abstract
Fluorinated sugar-1-phosphates are of emerging importance as intermediates in the chemical and biocatalytic synthesis of modified oligosaccharides, as well as probes for chemical biology. Here we present a systematic study of the activity of a wide range of anomeric sugar kinases (galacto- and N-acetylhexosamine kinases) against a panel of fluorinated monosaccharides, leading to the first examples of polyfluorinated substrates accepted by this class of enzymes. We have discovered four new N-acetylhexosamine kinases with a different substrate scope, thus expanding the number of homologs available in this subclass of kinases. Lastly, we have solved the crystal structure of a galactokinase in complex with 2-deoxy-2-fluoro galactose, giving insight into changes in the active site that may account for the specificity of the enzyme towards certain substrate analogues.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Pure (York) |
Date Deposited: | 04 Jun 2020 15:00 |
Last Modified: | 17 Dec 2024 00:16 |
Published Version: | https://doi.org/10.1016/j.chembiol.2020.06.005 |
Status: | Published online |
Refereed: | Yes |
Identification Number: | 10.1016/j.chembiol.2020.06.005 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:161506 |
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