title: Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28.
abstract: Anglerfish somatostatin-14 (SS-14) and somatostatin-28 (aSS-28) are derived from pro-somatostatin I (aPSS-I) and pro-somatostatin II (PSS-II), respectively. Purified yeast aspartic protease 3 (YAP3), was shown to cleave aPSS-I at the Arg81-Lys82 to yield SS-14 and Lys-1SS-14. In contrast, YAP3 cleaved aPSS-II only at the monobasic residue, Arg73 to yield aSS-28. Since the paired basic and monobasic sites are present in both precursors, the results indicate that the structure and conformation of these substrates dictate where cleavage occurs. Furthermore, the data show that YAP3 has specificity for both monobasic and paired basic residues.
authors.affiliation: Section on Cellular Neurobiology, National Institutes of Health, Bethesda, MD 20892.
authors.forename: N X
authors.initials: NX
authors.lastname: Cawley
authors.forename: B D
authors.initials: BD
authors.lastname: Noe
authors.forename: Y P
authors.initials: YP
authors.lastname: Loh
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000378:metabolism; D005399:Fishes; D007515:Islets of Langerhans / Q000378:metabolism; D007700:Kinetics; D011498:Protein Precursors / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013004:Somatostatin / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D053561:Somatostatin-28; D013379:Substrate Specificity; D013462:Sulfur Radioisotopes
chemical_list: D011498:Protein Precursors; D013462:Sulfur Radioisotopes; D013004:Somatostatin; C028456:prosomatostatin; D053561:Somatostatin-28; D016282:Aspartic Acid Endopeptidases; D003545:Cysteine