{"title":"Transglycosylases in peptidoglycan biosynthesis: advances in structure, function, and antimicrobial development","authors":"Xiao-Lin Zhang, Han Ding, Aoxin Guo, Xue-Wei Liu","doi":"10.1007/s11426-024-2601-y","DOIUrl":null,"url":null,"abstract":"<div><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.\n</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":772,"journal":{"name":"Science China Chemistry","volume":"68 9","pages":"4012 - 4024"},"PeriodicalIF":9.7000,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science China Chemistry","FirstCategoryId":"1","ListUrlMain":"https://link.springer.com/article/10.1007/s11426-024-2601-y","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
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.
期刊介绍:
Science China Chemistry, co-sponsored by the Chinese Academy of Sciences and the National Natural Science Foundation of China and published by Science China Press, publishes high-quality original research in both basic and applied chemistry. Indexed by Science Citation Index, it is a premier academic journal in the field.
Categories of articles include:
Highlights. Brief summaries and scholarly comments on recent research achievements in any field of chemistry.
Perspectives. Concise reports on thelatest chemistry trends of interest to scientists worldwide, including discussions of research breakthroughs and interpretations of important science and funding policies.
Reviews. In-depth summaries of representative results and achievements of the past 5–10 years in selected topics based on or closely related to the research expertise of the authors, providing a thorough assessment of the significance, current status, and future research directions of the field.