title: Multiple functions of pro-parts of aspartic proteinase zymogens.
abstract: The importance of aspartic proteinases in human pathophysiology continues to initiate extensive research. With burgeoning information on their biological functions and structures, the traditional view of the role of activation peptides of aspartic proteinases solely as inhibitors of the active site is changing. These peptide segments, or pro-parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. Consequently, the primary structures of pro-parts reflect these functions. We discuss guidelines for formation of hypotheses derived from comparing the physiological function of aspartic proteinases and sequences of their pro-parts.
authors.affiliation: Oklahoma Medical Research Foundation, Oklahoma City.
authors.forename: G
authors.initials: G
authors.lastname: Koelsch
authors.forename: M
authors.initials: M
authors.lastname: Mares
authors.forename: P
authors.initials: P
authors.lastname: Metcalf
authors.forename: M
authors.initials: M
authors.lastname: Fusek
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D016415:Sequence Alignment
chemical_list: D004792:Enzyme Precursors; D016282:Aspartic Acid Endopeptidases