Protein glycosylation is one of the most abundant and complex forms of posttranslational modification in mammalian cells. Metabolic chemical reporters (MCRs) have been indispensable for the visualization and identification of glycoproteins. Typically, MCRs are monosaccharide analogs that contain small bioorthogonal functional groups that are tolerated by cellular metabolism and become incorporated into glycoproteins. These functional groups can then be labeled using reactions, such as the copper(I) catalyzed azide-alkyne cycloaddition (CuAAC). Recently, we and others have demonstrated that most MCRs are not specific for one type of glycosylation. However, structural changes to the MCR could bias their incorporation into different glycans. Here I will present data on the metabolism and specific enzymatic turnover of four different MCRs that may explain their relative selectivity for different types of glycoproteins, with important implications for their application by the glycoprotein community.

Subtle structural changes effect the metabolic fate of four different chemical reporters of glycosylation

251st National Meeting (2016)

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