Lysozyme mode of action

Lysozyme Mode of Action of an Enzyme 1092 THE CHEMISTRY OF... Carbonic Anhydrase Shuttling the Protons 1094... 

A tremendous amount has been achieved by the application of X-ray crystallography in determining the three-dimensional structure of a-lactalbumin and lysozyme, and in the case of lysozyme, the mode of its catalytic action. Nevertheless, despite the tremendous advances, there are still areas of this mechanism that are not fully understood. This is especially true of the comparative mode of action of c-, g-, and phage-type lysozymes. 

Deslongchamps kindly provided us with his own view of the mechanistic path by which a-chymotrypsin and other serine proteases can hydrolyze secondary amides by stereoelectronic control (Fig. 4.7). Petkov et al. (119) also arrived at a similar proposal by studying the influence of the leaving group on the reactivity of specific anilides in a-chymotrypsin-catalyzed hydrolysis. Furthermore, the stereoelectronic control theory has been applied to the mode of action of ribonuclease A, staphylococcal nuclease and lysozyme (120). 

---