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

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

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...

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Bibliographic Details
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
Other Authors: School of Chemical and Biomedical Engineering
Format: Journal Article
Language:English
Published: 2024
Subjects:
Chemistry
Medicine, Health and Life Sciences
Anhydromuropeptide
Glycosylation
Glycosyl acceptor
Enzymes
Transglycosylase
Online Access:https://hdl.handle.net/10356/174229

Internet

https://hdl.handle.net/10356/174229

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