Abstract
ALTHOUGH the structure of hen's egg white lysozyme is known in great detail1–3, information about its mechanism of action is limited. Lysozyme has been shown to act as a glycosidase which hydrolyses β(1→4) N-acetylrnuramyl (MurNAc) linkages in bacterial cell walls and their oligo-saccharides, and β(1→4) N-acetylglucosaminyl (GlcNAc) linkages in chitin oligosaccharides4. To obtain more data on the specificity requirements and on the mechanism of action of lysozyme, we have investigated its action on oligosaccharides containing glucose (all β(1→4) linked). These included cellodextrins as well as oligosaccharides containing both glucose and N-acetylhexosamine residues. The results obtained provide information on the specificity requirements of subsites C and D in the active site of lysozyme and allow further insight to be gained into the role of strain as a major factor involved in lysozyme catalysis.
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ZEHAVI, U., POLLOCK, J., TEICHBERG, V. et al. Oligosaccharides containing Glucose as Substrates for Hen's Egg White Lysozyme. Nature 219, 1152–1154 (1968). https://doi.org/10.1038/2191152a0
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DOI: https://doi.org/10.1038/2191152a0
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