The versatility of proteolytic enzymes.
The growing realization of their physiological importance has generated renewed interest in the study of proteolytic enzymes. Modern methods of protein chemistry and molecular biology have revealed new insights into the protein and gene structure of a variety of protein precursors and their processing by limited proteolysis. Examples are given in this review for transmembrane processes and the role of signal peptidases of both eukaryotic and prokaryotic origin, the processing of prohormones and precursors of growth factors, protein components of blood coagulation, fibrinolysis, and of the complement system, and a group of granulocyte proteases, including the mast cell serine proteases. The relationship of homologous domains found in many of these proteases and their zymogens to protein evolution is a recurrent theme of this discussion.
D001777:Blood Coagulation; D002462:Cell Membrane / Q000201:enzymology; D003165:Complement System Proteins / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D005342:Fibrinolysis; D006133:Growth Substances / Q000378:metabolism; D006728:Hormones / Q000378:metabolism; D008565:Membrane Proteins; D010447:Peptide Hydrolases / Q000502:physiology*; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases
D006133:Growth Substances; D006728:Hormones; D008565:Membrane Proteins; D011498:Protein Precursors; D003165:Complement System Proteins; D010450:Endopeptidases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C026515:type I signal peptidase