GlcNAc-1,6-anhydro-MurNAc moiety affords unusual glycosyl acceptor that terminates peptidoglycan elongation

• Main Authors: Zhang, Xiao-Lin, Báti, Gábor, Li, Chenyu, Guo, Aoxin, Yeo, Claresta, Ding, Han, Pal, Kumar Bhaskar, Xu, Yuan, Qiao, Yuan, Liu, Xue-Wei
• 其他作者: School of Chemical and Biomedical Engineering
• 格式: Article
• 語言: English
• 出版: 2024
• 主題: Chemistry; Medicine, Health and Life Sciences; Anhydromuropeptide; Glycosylation; Glycosyl acceptor; Enzymes; Transglycosylase
• 在線閱讀: https://hdl.handle.net/10356/174229

Peptidoglycan (PG), an essential exoskeletal polymer in bacteria, is a well-known antibiotic target. PG polymerization requires the action of bacterial transglycosylases (TGases), which couple the incoming glycosyl acceptor to the donor. Interfering with the TGase activity can interrupt the PG assem...