Lysozyme is an antibacterial enzyme that hydrolyzes polysaccharides in bacterial cell walls. It also catalyzes the hydrolysis of a β-1,4-linked hexasaccharide oligomer of N-acefylglucosamine into a teffasaccharide and a disaccharide with retention a:f
stereochemisffry; as shown in Fig. P26,74, The active site of lysoryme runs through the enzyme at the junction of the two domains (Fig. 26.10, p. 131 1). Near one end of the active site are two aspartic acid residues, Asp35 and Asp52, which are believed to be essential residues involved in the catalysis of hydrolysis. The pKa values of the carboxylic acid groups in the side chains of these residues are about 5.0 and 3.5, respectively, The enzyme functions optimally at pH = 5.
Treatment of lysozyme with triethyloxonium tetrafluoroborate results in a reaction of the carboxylic acid group of Asp52 that completely eliminates enzyme activity. What is this reaction? In the light of the mechanism you proposed in account for the effect of this reaction on enzyme activity.