Bacterial peptidoglycan (murein) hydrolases.
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 beta-lactamase.
Vollmer
Waldemar
W
Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne, UK. w.vollmer@ncl.ac.uk
Joris
Bernard
B
Charlier
Paulette
P
Foster
Simon
S
D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000145:classification* / Q000502:physiology*; D001433:Bacteriolysis; D002455:Cell Division; D002473:Cell Wall / Q000201:enzymology / Q000378:metabolism; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000145:classification* / Q000502:physiology*; D010457:Peptidoglycan / Q000378:metabolism; D013171:Spores, Bacterial / Q000201:enzymology
D001426:Bacterial Proteins; D010457:Peptidoglycan; D009238:N-Acetylmuramoyl-L-alanine Amidase