Specific and Irreversible Inhibition of Lysozyme by 2′,3′-Epoxypropyl β-Glycosides of N-Acetyl-D-glucosamine Oligomers

Abstract

THE structure and properties of hen's egg white lysozyme and of the lysozyme–inhibitor complexes are known in detail^1,2, but there is no direct evidence as to which amino-acid residues are involved in the bond breaking step. Specific chemical modification of the active site residues is an obvious approach to the problem, arid we describe here an attempt to design specific inhibitors of lysozyme, using the affinity labelling principle^3,4. Because the side chains of amino-acid residues Glu 35 and Asp 52 have been proposed as the catalytically active groups in lysozyme², we have prepared potential lysozyme inhibitors which can react with carboxyl functions, and have investigated their effect on the enzyme.