FROM GROWTH TO AUTOLYSIS - THE MUREIN HYDROLASES IN ESCHERICHIA-COLI

Murein hydrolases cleave bonds in the bacterial exoskeleton, the murein (peptidoglycan) sacculus, a covalently closed bag-shaped polymer made of glycan strands that are crosslinked by peptides. During growth and division of a bacterial cell, these enzymes are involved in the controlled metabolism of the murein sacculus. Murein hydrolases are believed to function as pacemaker enzymes for the enlargement of the murein sacculus since opening of bonds in the murein net is needed to allow the insertion of new subunits into the sacculus. Furthermore, they are responsible for splitting the septum during cell division. The murein turnover products that are released during growth are further degraded by these hydrolases to products that can be recycled by the biosynthetic enzymes. As potentially suicidal (autolytic) enzymes, murein hydrolases must be strictly controlled by the cell, Inhibition of murein synthesis, for example by penicillin, triggers an unbalanced action of murein hydrolases causing bacteriolysis. In Escherichia coli, 14 different murein hydrolases have so far been identified, including N-acetylmuramyl-L-alanine amidases, DD-endopeptidases, DD-carboxypeptidases, LD-carboxypeptidases, and N-acetylglucosaminidases. In addition, lysozyme-like enzymes, called ''lytic transglycosylases,'' produce (1-->6)-anhydromuramic acid derivatives by an intramolecular transglycosylation reaction.