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Purified yeast aspartic protease 3 cleaves anglerfish pro‐somatostatin I and II at di‐ and monobasic sites to generate somatostatin‐14 and ‐28
Author(s) -
Cawley Niamh X.,
Noe Bryan D.,
Loh Y.Peng
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80648-e
Subject(s) - monobasic acid , somatostatin , protease , biochemistry , chemistry , yeast , enzyme , biology , endocrinology , organic chemistry
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 Arg 18 ‐Lys 82 to yield SS‐14 and Lys −1 SS‐H. In contrast, YAP3 cleaved aPSS‐II only at the monobasic residue. Arg 73 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.