An iterative glycosyltransferase EntS catalyzes transfer and extension of O- and S-linked monosaccharide in enterocin 96

Glycobiology
Rupa Nagar, Alka Rao

Abstract

Glycosyltransferases are essential tools for in vitro glycoengineering. Bacteria harbor an unexplored variety of protein glycosyltransferases. Here, we describe a peptide glycosyltransferase (EntS) encoded by ORF0417 of Enterococcus faecalis TX0104. EntS di-glycosylates linear peptide of enterocin 96 - a known antibacterial, in vitro. It is capable of transferring as well as extending the glycan onto the peptide in an iterative sequential dissociative manner. It can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(β)Glc/Gal(-O/S)Ser/Thr/Cys, in one pot. Using EntS generated glycovariants of enterocin 96 peptide, size and identity of the glycan are found to influence bioactivity of the peptide. The study identifies EntS as an enzyme worth pursuing, for in vitro peptide glycoengineering.

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Citations

Jan 12, 2019·Critical Reviews in Microbiology·Aadil Hussain BhatKiran Ambatipudi
Oct 31, 2019·Nucleic Acids Research·Krishnaveni PalaniappanNigel J Mouncey
Jul 21, 2021·Cell Chemical Biology·Daisuke FujinamiWilfred A van der Donk
Sep 6, 2018·ACS Chemical Biology·Hengqian RenHuimin Zhao

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