The Binding of Oligosaccharides Containing N-Acetylglucosamine and N-Acetylmuramic Acid to Lysozyme

Abstract

Abstract The association constants with lysozyme of several saccharides containing N-acetyl-d-glucosamine and N-acetylmuramic acid, have been determined by fluorescence spectroscopy or, in one case, by equilibrium dialysis experiments. The association data may be understood on the assumption that the active site of lysozyme consists of a number of subsites binding individual 2-acetamido-2-deoxyglucopyranose rings. On the basis of these data, we have drawn detailed conclusions about the specificity of the individual subsites and their contributions to the total binding energy of oligosaccharide substrates and inhibitors. These conclusions are consistent with, and offer further support of, the mechanism of lysozyme action deduced by Phillips and his coworkers on the basis of x-ray crystallographic studies.