Yapsin1: Structure, biosynthesis, and specificity

Advances in Experimental Medicine and Biology

Volumn 436, Issue , 1998, Pages 315-319

  Olsen, Vicki ^a   Cawley, Niamh X ^a   Loh, Y Peng ^a,b  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEINASE; ENZYME; GENE PRODUCT; NUCLEOTIDE; PHEROMONE;

CONFERENCE PAPER; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; HYDROPHOBICITY; MAMMAL; MOLECULAR CLONING; PHENOTYPE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

MAMMALIA;

EID: 0031944726     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-5373-1_42     Document Type: Conference Paper

References (14)

1. M. Egel-Mitani, H.P. Flygenring and M. Trier Hansen, A novel aspartyl protease allowing KEX2-independent MFα propheromone processing in yeast. Yeast 6:127 (1990)
2. H. Komano and R.S. Fuller, Shared functions in vivo of a glycosyl- phosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing Kex2 in yeast. Proc. Natl. Acad. Sci. USA 92:10752 (1995)
3. Y.P. Loh, D.C. Parish and R. Tuteja, Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles. J.Biol.Chem. 260:7194 (1985)
4. N.X. Cawley, L.-P. Pu and Y.P. Loh, Immunological identification and localization of yeast aspartic protease 3-like prohormone-processing enzymes in mammalian brain and pituitary. Endocrinology 137:5135 (1996)
5. B.M. Dunn, M. Jimenez, B.F. Parten, M.J, Valler, C.E. Rolph and J. Kay, A systematic series of synthetic chromophoric substrates for aspartic proteases. Biochem. J. 237:899 (1986)
6. J. Ash, M. Dominguez, J.J.M. Bergeron, D.Y. Thomas and Y. Bourbonnais, The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol- anchored protein that localizes to the plasma membrane. J. Biol. Chem. 270:20847 (1995)
7. N.X. Cawley, M. Wong, L.-P. Pu, W. Tam and Y.P. Loh, Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminal tail: characterization of secreted YAP3p. Biochem. 34:7430 (1995)
8. V.L. MacKay, J. Armstrong, C. Yip, S. Welch, K. Walker, S. Osborn, P. Sheppard and J. Forstrom, Characterization of the BAR proteinase, an extracellular enzyme from the yeast Saccharomyces cerevisiae, in: Structure and Function of the Aspartic Proteinases, B. M. Dunn, ed., pp. 161, Plenum Press:New York, NY (1991)
9. A. Azaryan, M. Wong, T.C. Friedman, N.X. Cawley, F.E. Estivarez, H.-C. Chen and Y.P. Loh, Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme. J.Biol.Chem. 268:11968 (1993)
10. J.B. Cooper, G. Khan, G. Taylor, I.J. Tickle and T.L. Blundell, X-ray analyses of Aspartic proteinases II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 Å resolution. J. Mol. Biol. 214:199 (1990)
11. N.X. Cawley, H.-C. Chen, M.C. Beinfeld and Y.P. Loh, Specificity and kinetic studies on the cleavage of various prohormone mono- and paired basic residue sites by yeast aspartic protease 3. J. Biol. Chem. 271:4168 (1996)
12. N.X. Cawley, B.D. Noe and Y.P. Loh, Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28. FEBS Lett. 332:273 (1993)
13. E.C. Ledgerwood, S.O. Brennan, N.X. Cawley, Y.P. Loh and P.M. George, Yeast aspartic protease 3 (Yap3) prefers substrates with basic residues in the P2, P1 and P2 positions. FEBS Lett. 383:67 (1996)
14. V. Olsen, A putative prohormone convertase from Saccharomyces cerevisiae. Characterization of biosynthesis and cellular localization of the YAP3 gene product. M.S. Thesis, University of Copenhagen, Denmark (1994)