Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d -Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition
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Glucokinase phosphorylated a series of C-1 fluorinated [alpha]-d-gluco-heptuloses. These phosphorylated products were discovered to be inhibitors of [alpha]-phosphomannomutase/phosphoglucomutase ([alpha]PMM/PGM) and [beta]-phosphoglucomutase ([beta]PGM). Inhibition potency with both mutases inversely correlated to the degree of fluorination. Structural analysis with [alpha]PMM demonstrated the inhibitor binding to the active site, with the phosphate in the phosphate binding site and the anomeric hydroxyl directed to the catalytic site.
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