How serpins recognize and inhibit serine proteases

Structural and mechanistic insight into how antibodies inhibit serine proteases.

Antibodies display great versatility in protein interactions and have become important therapeutic agents for a variety of human diseases. Their ability to discriminate between highly conserved sequences could be of great use for therapeutic approaches that target proteases, for which structural features are conserved among family members. Recent crystal structures of antibody-protease complexe...

Serine Proteases of Parasitic Helminths

Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization. A number of serine proteases have been identified in parasitic helminths that have putative roles in parasite development an...

Detection of the Keratinolytic Activity of Agriculture and Mount Barker Strain Dermatophilus congolensis Serine Proteases.

Inhibition of Elastase and Other Serine Proteases

The N-acylsaccharins and N-acylbenzoisothiazolinones form a new class of acylating inhibitors of the serine proteases with a broad spectrum of activity. However, they are unique in that they are able to differentiate between various serine proteases because of the differential stability of the presumptive acylenzyme formed. Furoyl saccharin was the best studied among this class of inhibitors. W...

Inhibition of serine proteases by arylboronic acids.

Arylboronic acids were found to be strong competitive inhibitors of subtilisin and chymotrypsin. The binding constants are strongly pH dependent and give a Hammett-type plot with a slope of -0.885. The pH dependence, the Hammett plot, and nmr model-system studies indicate that inhibition is due to electron-pair donation by the active site histidine to the bound inhibitor.