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
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
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.