Lytic transglycosylases: bacterial space-making autolysins

Int J Biochem Cell Biol. 2008;40(4):586-91. doi: 10.1016/j.biocel.2007.03.018. Epub 2007 Mar 30.


Lytic transglycosylases are an important class of bacterial enzymes that act on peptidoglycan with the same substrate specificity as lysozyme. Unlike the latter enzymes, however, the lytic transglycosylases are not hydrolases but instead cleave the glycosidic linkage between N-actetylmuramoyl and N-acetylglucosaminyl residues with the concomitant formation of a 1,6-anydromuramoyl product. They are ubiquitous in bacteria which produce a compliment of different forms that are responsible for creating space within the peptidoglycan sacculus for its biosynthesis and recycling, cell division, and the insertion of cell-envelope spanning structures, such as flagella and secretion systems. As well, the lytic transglyosylases may have a role in pathogenesis of some bacterial species. Given their important role in bacterial cell wall metabolism, the lytic transglycosylases may present an attractive new target for the development of broad-spectrum antibiotics.

Publication types

  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Cell Wall / metabolism
  • Glycosyltransferases / chemistry
  • Glycosyltransferases / genetics
  • Glycosyltransferases / metabolism*
  • Molecular Structure
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry
  • N-Acetylmuramoyl-L-alanine Amidase / genetics
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism*
  • Peptidoglycan / metabolism


  • Bacterial Proteins
  • Peptidoglycan
  • Glycosyltransferases
  • N-Acetylmuramoyl-L-alanine Amidase