The autolytic peptidoglycan hydrolases of Streptococcus faecium

Streptococcus faecium ATCC 9790 possesses two peptidoglycan hydrolase activities. The first enzyme, an N-acetylmuramoylhydrolase, has been purified and has been shown to be a glucoenzyme. Studies of hydrolysis of soluble, linear uncross-linked peptidoglycan chains showed that the enzyme bound strongly to the non-reducing ends of the chains and then sequentially (processively) hydrolysed susceptible bonds in that chain. The second peptidoglycan hydrolase does not appear to be a glycoprotein and differs from the first enzyme in substrate specificity and mechanism of hydrolysis. The presence of two partially redundant activities which may play different roles in surface growth and division could, at least in part, explain previous difficulties in obtaining mutants which completely lack autolytic activity.