Editor: Jacques Coyette
Bacterial peptidoglycan (murein) hydrolases
Article first published online: 11 FEB 2008
© 2008 Federation of European Microbiological Societies
FEMS Microbiology Reviews
Volume 32, Issue 2, pages 259–286, March 2008
How to Cite
Vollmer, W., Joris, B., Charlier, P. and Foster, S. (2008), Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiology Reviews, 32: 259–286. doi: 10.1111/j.1574-6976.2007.00099.x
- Issue published online: 11 FEB 2008
- Article first published online: 11 FEB 2008
- Received 10 October 2007; revised 16 November 2007; accepted 30 November 2007.First published online February 2008.
- peptidoglycan hydrolase;
- lytic transglycosylase;
Most bacteria have multiple peptidoglycan hydrolases capable of cleaving covalent bonds in peptidoglycan sacculi or its fragments. An overview of the different classes of peptidoglycan hydrolases and their cleavage sites is provided. The physiological functions of these enzymes include the regulation of cell wall growth, the turnover of peptidoglycan during growth, the separation of daughter cells during cell division and autolysis. Specialized hydrolases enlarge the pores in the peptidoglycan for the assembly of large trans-envelope complexes (pili, flagella, secretion systems), or they specifically cleave peptidoglycan during sporulation or spore germination. Moreover, peptidoglycan hydrolases are involved in lysis phenomena such as fratricide or developmental lysis occurring in bacterial populations. We will also review the current view on the regulation of autolysins and on the role of cytoplasm hydrolases in peptidoglycan recycling and induction of β-lactamase.