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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 390, Issue 3

Issues

Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties

Olga Hrušková-Heidingsfeldová
  • 1Gilead Sciences Research Center, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ-166 10 Prague 6, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jiří Dostál
  • 2Gilead Sciences Research Center, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ-166 10 Prague 6, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Filip Majer
  • Present address: 1st Faculty of Medicine, Institute of Inherited Metabolic Disorders, Charles University, Ke Karlovu 2, CZ-128 53 Prague 2, Czech Republic.
    3Gilead Sciences Research Center, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ-166 10 Prague 6, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jana Havlíková
  • 4Gilead Sciences Research Center, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ-166 10 Prague 6, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Martin Hradilek
  • 5Gilead Sciences Research Center, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ-166 10 Prague 6, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Iva Pichová
  • 6Gilead Sciences Research Center, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, CZ-166 10 Prague 6, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-01-23 | DOI: https://doi.org/10.1515/BC.2009.034

Abstract

Secreted aspartic proteinases (Sap) play a role in the virulence of pathogenic Candida spp. Candida parapsilosis possesses three genes encoding these enzymes: SAPP1, SAPP2, and SAPP3. We analyzed the expression of the SAPP1 and SAPP2 genes and the production of Sapp1p and Sapp2p proteinases in the presence of different nitrogen sources. While the SAPP2 transcript was present under all of the conditions tested, expression of SAPP1 was induced only by the presence of exogenous protein as the sole nitrogen source. The concentration of Sapp1p in the medium upon induction was at least one order of magnitude higher than the concentration of Sapp2p in all media tested in this study. Enzymological characterization of purified Sapp1p and Sapp2p demonstrated that Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than Sapp1p. Homology models of Sapp1p and Sapp2p revealed structural motifs that may be responsible for the differences between these two enzymes. Our results indicate that C. parapsilosis secretes a low level of Sapp2p proteinase with narrow substrate specificity and low proteolytic activity under most conditions, while expression and secretion of a higher amount of catalytically efficient Sapp1p enzymes is triggered in the presence of exogenous protein serving as a nitrogen source.

Keywords: aspartic proteinase; Candida parapsilosis; catalytic activity; gene regulation; SAPP1, SAPP2

About the article

Corresponding author


Received: 2008-08-27

Accepted: 2008-12-11

Published Online: 2009-01-23

Published in Print: 2009-03-01


Citation Information: Biological Chemistry, Volume 390, Issue 3, Pages 259–268, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.034.

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