Abstract
The natural substrate of lysozyme is the rigid layer of bacterial cell walls, the murein (peptidoglycan), which is a gigantic polymer of (GlcNAc-MurNAc)n polysaccharide strands crosslinked through short peptide bridges at the lactyl groups of the muramic acid residues. Thus, lysozyme lyses bacteria by degrading their protective exoskeleton, the murein sacculus. The high molecular weight murein is thereby hydrolysed to low molecular weight muropeptides, a process that can be followed quantitatively by different methods. However, due to the insolubility of the murein sacculus, the enzyme kinetics are rather complex. Therefore, a variety of different low molecular weight substrates have been prepared, both murein degradation products and synthetic compounds. These substrates allow a better characterization of the binding and catalytic mechanism of lysozyme. In addition, they are used in various photometric, isotopic and immunological lysozyme assays.
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