PURIFIED YEAST ASPARTIC PROTEASE-3 CLEAVES ANGLERFISH PRO-SOMATOSTATIN-I AND PRO-SOMATOSTATIN-II AT DIBASIC AND MONOBASIC SITES TO GENERATESOMATOSTATIN-14 AND SOMATOSTATIN-28

Citation
Nx. Cawley et al., PURIFIED YEAST ASPARTIC PROTEASE-3 CLEAVES ANGLERFISH PRO-SOMATOSTATIN-I AND PRO-SOMATOSTATIN-II AT DIBASIC AND MONOBASIC SITES TO GENERATESOMATOSTATIN-14 AND SOMATOSTATIN-28, FEBS letters, 332(3), 1993, pp. 273-276
Citations number
23
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
332
Issue
3
Year of publication
1993
Pages
273 - 276
Database
ISI
SICI code
0014-5793(1993)332:3<273:PYAPCA>2.0.ZU;2-A
Abstract
Anglerfish somatostatin-14 (SS-14) and somatostatin-28 (aSS-28) are de rived 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 confor mation of these substrates dictate where cleavage occurs. Furthermore, the data show that YAP3 has specificity for both monobasic and paired basic residues.