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Most bacteria are stabilized by the polymeric glycopeptide murein (peptidoglycan), a network of glycan strands interlinked by short peptides (see Fig. 1). The murein completely encloses the cell, thereby forming a kind of bag-shaped exoskeleton called a sacculus (Weidel & Pelzer, 1964; Mirelman, 1979; Tipper & Wright, 1979; Rogers et al., 1980). Expansion of the wall during bacterial growth and splitting of the septum for cell separation call for enzymes that cleave covalent bonds within the murein sacculus. Thus, bacterial growth depends on murein hydrolases, a class of enzymes ubiquitous among bacteria (Ghuysen, 1968). Such simple statements, however, belie the complexity and remarkable activity of these enzymes on the bacterial surface. New insight gained over the past decade has led to an emerging picture of a rather dynamic state of the bacterial sacculus in which the murein net is continuously subjected to intense hydrolytic attack, as indicated by insertion of new material, and remodelling and release of aged material. In addition to acting as pacemaker and spacemaker enzymes for cell wall growth (Weidel & Pelzer, 1964; Tomasz, 1983, 1984) some of the murein hydrolases can act as autolysins, thereby representing potential suicide enzymes. This life and death dichotomy of function demands efficient and strict regulation of murein hydrolase activity, a highly sophisticated physiological task. The enzymes, which must be controlled at their extracytoplasmic location, are required to act coordinately to govern orderly growth and division of the cell with its specific shape preserved. Antibiotics such as penicillin induce bacteriolysis by interfering with the control of the endogenous autolytic enzymes (Tomasz & Holtje, 1977 ; Tomasz, 1979), indicating the major chemotherapeutic relevance of this class of enzymes. Fine tuning of 1 1 . . . GlcNAc-MurNAc-GlcNAc . + .

The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo