Bacteria produce several peptidoglycan hydrolases (PGHs). There are at least five types of PGHs: endo-β-N-acetylglucosaminidase, endo-β-N-acetylmuraminidase, N-acetylmuramyl-L-alanine-amidase, endopeptidase and transglycosylase; each known for the specific bond they split in the cell wall (1,19). They are ubiquitous in bacteria and show functions in restructuring the cell wall where they have many important roles in cell wall metabolism including nicking peptidoglycan for insertion of a new peptidoglycan monomer, cell division, cell separation, and cell wall turnover (1,19,26). Many PGHs are termed bacteriolytic because the action of the enzyme often leads to bacterial cell lysis. Some enzymes are able to disintegrate their own peptidoglycan saccules when the cells are placed in unfavorable conditions; and such enzymes are called autolysins.Streptococci are Gram-positive bacteria where individual cells are connected with each other forming a chain morphology. Among the streptococci, S. pneumoniae, the leading cause of pneumonia, blood stream infections and otitis media, is the most extensively studied concerning the biochemistry and physiological functions of the PGHs. S. pneumoniae produces at least three types of PGHs: LytA amidase (16), LytB endo-β-N-acetylglucosaminidase (4, 7) and LytC lysozyme (6). Their roles in cell separation and viru-