Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme.

The latent form of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium ATCC 9790 was purified to near homogeneity by affinity chromatography on concanavalin A-Sepharose 4B. The latent enzyme had Mr approximately 130,000 on sodium dodecyl sulfate-gel electrophoresis. Upon proteinase treatment (trypsin or endogenous proteinase), the latent form is converted to an active form Mr approximately 87,000. The enzyme was shown to be glycoprotein, containing monomeric and oligomeric glucose substituents. Some of the substrate specificity requirements of this enzyme are described.