Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu
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nihms-1849878.pdf
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Accepted version
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825.23 KB
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Author(s)
Anderson, Alyssa J
Seebald, Leah M
Arbour, Christine A
Imperiali, Barbara
Date Issued
November 18, 2022
Journal
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
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1021/acschembio.2c00648
