title: Proteolytic processing and regulation.
abstract: Many proteins, particularly proteolytic enzymes, protein hormones and neuropeptides are synthesized as inactive precursors that undergo posttranslational processing by proteolytic enzymes. The roots of current knowledge go back to the early observations of the activation of zymogens. A major advance followed the discovery of the polypreprotein, pre-pro-opiomelanolcortin and of proinsulin, and the characterization of the mammalian processing prohormone enzyme as members of the multidomain yeast kexin family. More recent applications of methods of molecular biology have greatly advanced our understanding of the nature and mode of action of these proteases.
authors.affiliation: Department of Biochemistry, University of Washington, Seattle.
authors.forename: H
authors.initials: H
authors.lastname: Neurath
mesh_terms: D010450:Endopeptidases / Q000378:metabolism*; D043484:Proprotein Convertases; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000378:metabolism; D013381:Subtilisins
chemical_list: D011498:Protein Precursors; D029701:Saccharomyces cerevisiae Proteins; D010450:Endopeptidases; D043484:Proprotein Convertases; D012697:Serine Endopeptidases; D013381:Subtilisins; C058751:KEX2 protein, S cerevisiae