Literature DB >> 8104828

Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28.

N X Cawley1, B D Noe, Y P Loh.   

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.

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Year:  1993        PMID: 8104828     DOI: 10.1016/0014-5793(93)80648-e

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Identification and characterization of Saccharomyces cerevisiae yapsin 3, a new member of the yapsin family of aspartic proteases encoded by the YPS3 gene.

Authors:  V Olsen; N X Cawley; J Brandt; M Egel-Mitani; Y P Loh
Journal:  Biochem J       Date:  1999-04-15       Impact factor: 3.857

2.  Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway.

Authors:  K S Copley; S M Alm; D A Schooley; W E Courchesne
Journal:  Biochem J       Date:  1998-03-15       Impact factor: 3.857

3.  Temperature-induced conformational changes in prosomatostatin-II: implications for processing.

Authors:  J Mitra; X Tang; S C Almo; D Shields
Journal:  Biochem J       Date:  1998-08-15       Impact factor: 3.857

4.  N-terminal entrance loop of yeast Yps1 and O-glycosylation of substrates are determinant factors controlling the shedding activity of this GPI-anchored endopeptidase.

Authors:  Alexandre K Dubé; Marc Bélanger; Isabelle Gagnon-Arsenault; Yves Bourbonnais
Journal:  BMC Microbiol       Date:  2015-02-26       Impact factor: 3.605

  4 in total

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