A uniform treatment of the four protease groups and a discussion of the differences and similarities in their action is presented in this important new publication. Serine, cysteine, aspartate, and zinc proteases are systematically discussed by nomenclature, evolution, specificity and their regulatory role. The chemistry of the peptide bond, including the catalysis of ester and peptide hydrolyses, is explained.
For each protease group the emphasis is placed on the structure and function. Kinetics, enzyme modifications, isotope effects, subzero temperature investigations, nuclear magnetic resonance measurements, X-ray diffraction data, binding of transition-state analogs, zymogen activation, and site-specific mutagenesis are combined to rationalize the action of proteases. Both natural and synthetic inhibitors are considered because of their importance in mechanistic studies and drug design.
For each protease group the emphasis is placed on the structure and function. Kinetics, enzyme modifications, isotope effects, subzero temperature investigations, nuclear magnetic resonance measurements, X-ray diffraction data, binding of transition-state analogs, zymogen activation, and site-specific mutagenesis are combined to rationalize the action of proteases. Both natural and synthetic inhibitors are considered because of their importance in mechanistic studies and drug design.
