Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu
Author(s)
Anderson, Alyssa J; Seebald, Leah M; Arbour, Christine A; Imperiali, Barbara
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Monotopic phosphoglycosyl transferase enzymes (monoPGTs) initiate the assembly of prokaryotic glycoconjugates essential for bacterial survival and proliferation. MonoPGTs belong to an expansive superfamily with a diverse and richly annotated sequence space; however, the biochemical roles of most monoPGTs in glycoconjugate biosynthesis pathways remain elusive. To better understand these critical enzymes, we have implemented activity-based protein profiling (ABPP) probes as protein-centric, membrane protein compatible tools that lay the groundwork for understanding the activity and regulation of the monoPGT superfamily from a cellular proteome. With straightforward gel-based readouts, we demonstrate robust, covalent labeling at the active site of various representative monoPGTs from cell membrane fractions using 3-phenyl-2H-azirine probes.
Date issued
2022-11-18Department
Massachusetts Institute of Technology. Department of BiologyJournal
ACS Chemical Biology
Publisher
American Chemical Society (ACS)
Citation
Anderson, Alyssa J, Seebald, Leah M, Arbour, Christine A and Imperiali, Barbara. 2022. "Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu." ACS Chemical Biology, 17 (11).
Version: Author's final manuscript