Scholarlink

<p>Peptidoglycan (PG), the essential exoskeleton in most bacteria, is synthesized through the action of bacterial transglycosylases (TGases), positioning these enzymes as elegant and desirable targets for antibiotic discovery. This review covers the major TGases involved in PG biogenesis, including TGases from the glycosyltransferase family 51 (GT51) and the newly discovered shape, elongation, division, sporulation (SEDS) family. We discuss the distinct roles of these two TGases during PG synthesis and emphasize the structural and catalytic differences, highlighting their coordination in PG assembly. Moreover, we summarize recent advances in TGase-involved antimicrobial strategies, including substrate-mimicking TGase inhibitors, PG terminators, and TGase-related immunological therapy targeting TGase from the GT51 family, and the first non-substrate-like TGase inhibitor against the SEDS protein. These valuable insights pave the way for the further development of novel TGase-related antimicrobial agents.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Transglycosylases in peptidoglycan biosynthesis: advances in structure, function, and antimicrobial development

  • 期刊论文

  • 发表日期：

    2025年7月1日

查看全文
  • Xiao-Lin Zhang,
  • Han Ding,
  • Aoxin Guo,
  • Xue-Wei Liu

摘要

Peptidoglycan (PG), the essential exoskeleton in most bacteria, is synthesized through the action of bacterial transglycosylases (TGases), positioning these enzymes as elegant and desirable targets for antibiotic discovery. This review covers the major TGases involved in PG biogenesis, including TGases from the glycosyltransferase family 51 (GT51) and the newly discovered shape, elongation, division, sporulation (SEDS) family. We discuss the distinct roles of these two TGases during PG synthesis and emphasize the structural and catalytic differences, highlighting their coordination in PG assembly. Moreover, we summarize recent advances in TGase-involved antimicrobial strategies, including substrate-mimicking TGase inhibitors, PG terminators, and TGase-related immunological therapy targeting TGase from the GT51 family, and the first non-substrate-like TGase inhibitor against the SEDS protein. These valuable insights pave the way for the further development of novel TGase-related antimicrobial agents.