Jump to ContentJump to Main Navigation
Show Summary Details
More options …

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

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 393, Issue 12

Issues

Gingipain aminopeptidase activities in Porphyromonas gingivalis

Florian Veillard
  • Corresponding author
  • Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY, USA
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Barbara Potempa
  • Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marcin Poreba
  • Division of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wroclaw, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marcin Drag
  • Division of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Technology, Wroclaw, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jan Potempa
  • Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY, USA
  • Faculty of Biochemistry, Department of Microbiology, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2012-11-13 | DOI: https://doi.org/10.1515/hsz-2012-0222

Abstract

Bestatin, a specific inhibitor of metalloaminopeptidases, inhibits the growth of Porphyromonas gingivalis. To identify its target enzyme, a library of fluorescent substrates was used but no metalloaminopeptidase activity was found. The aminopeptidase activity of P. gingivalis was bestatin-insensitive and directed exclusively toward N-terminal arginine and lysine substrates. Class-specific inhibitors and gingipain-null mutants showed that gingipains were the only enzymes responsible for this activity. The kinetic constants obtained for Rgps were comparable to those of human aminopeptidases but Kgp aminopeptidase activity was weaker. This finding reveals a new role for gingipains as aminopeptidases in the degradation of proteins and peptides in P. gingivalis.

Keywords: periodontitis; proteolysis; proteolytic enzyme

About the article

Corresponding author: Florian Veillard, Oral Health and Systemic Diseases Research Group, University of Louisville School of Dentistry, Louisville, KY, USA


Received: 2012-06-05

Accepted: 2012-08-13

Published Online: 2012-11-13

Published in Print: 2012-12-01


Citation Information: Biological Chemistry, Volume 393, Issue 12, Pages 1471–1476, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2012-0222.

Export Citation

©2012 by Walter de Gruyter Berlin Boston.Get Permission

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Florian Veillard, Maryta Sztukowska, Zuzanna Nowakowska, Danuta Mizgalska, Ida B. Thøgersen, Jan J. Enghild, Matthew Bogyo, Barbara Potempa, Ky-Anh Nguyen, and Jan Potempa
Biochimie, 2019
[2]
Brian W. Bainbridge, Takanori Hirano, Nicole Grieshaber, Mary E. Davey, and G. A. O'Toole
Journal of Bacteriology, 2015, Volume 197, Number 7, Page 1208
[3]
Dominika Staniec, Miroslaw Ksiazek, Ida B. Thøgersen, Jan J. Enghild, Aneta Sroka, Danuta Bryzek, Matthew Bogyo, Magnus Abrahamson, and Jan Potempa
Journal of Biological Chemistry, 2015, Volume 290, Number 45, Page 27248
[4]
Tania Køllgaard, Christian Enevold, Klaus Bendtzen, Peter R. Hansen, Michael Givskov, Palle Holmstrup, Claus H. Nielsen, and Salomon Amar
PLOS ONE, 2017, Volume 12, Number 2, Page e0172773
[5]
Zachary D. Moye, Kornelija Valiuskyte, Floyd E. Dewhirst, Frank C. Nichols, and Mary E. Davey
Frontiers in Microbiology, 2016, Volume 7
[6]
V. Friedrich, C. Gruber, I. Nimeth, S. Pabinger, G. Sekot, G. Posch, F. Altmann, P. Messner, O. Andrukhov, and C. Schäffer
Molecular Oral Microbiology, 2015, Volume 30, Number 6, Page 451
[7]
Florian Veillard, Maryta Sztukowska, Danuta Mizgalska, Mirosław Ksiazek, John Houston, Barbara Potempa, Jan J. Enghild, Ida B. Thogersen, F. Xavier Gomis-Rüth, Ky-Anh Nguyen, and Jan Potempa
Biochimica et Biophysica Acta (BBA) - General Subjects, 2013, Volume 1830, Number 8, Page 4218

Comments (0)

Please log in or register to comment.
Log in