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Publication Abstract from PubMed

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-fluorogalactose, giving insight into changes in the active site that may account for the specificity of the enzyme toward certain substrate analogs.

Profiling Substrate Promiscuity of Wild-Type Sugar Kinases for Multi-fluorinated Monosaccharides.,Keenan T, Parmeggiani F, Malassis J, Fontenelle CQ, Vendeville JB, Offen W, Both P, Huang K, Marchesi A, Heyam A, Young C, Charnock SJ, Davies GJ, Linclau B, Flitsch SL, Fascione MA Cell Chem Biol. 2020 Jun 30. pii: S2451-9456(20)30228-2. doi:, 10.1016/j.chembiol.2020.06.005. PMID:32619452^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.