Abstract
This chapter examines families of serine peptidases. Serine peptidases are found in viruses, bacteria, and eukaryotes. They include exopeptidases, endopeptidases, oligopeptidases, and omega peptidases. On the basis of three-dimensional structures, most of the serine peptidase families can be grouped together into about six clans that may have common ancestors. The structures are known for members of four of the clans, chymotrypsin, subtilisin, carboxypeptidase C, and Escherichia D-Ala-D-Ala peptidase A. The peptidases of chymotrypsin, subtilisin, and carboxypeptidase C clans have a common “catalytic triad” of three amino acids—namely, serine (nucleophile), aspartate (electrophile), and histidine (base). The geometric orientations of these are closely similar between families; however the protein folds are quite different. The arrangements of the catalytic residues in the linear sequences of members of the various families commonly reflect their relationships at the clan level. The members of the chymotrypsin family are almost entirely confined to animals. 10 families are included in chymotrypsin clan (SA), and all the active members of these families are endopeptidases. The order of catalytic residues in the polypeptide chain in clan SA is His/Asp/Ser.