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

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 383, Issue 7-8 (Aug 2002)

Issues

Role of the Prosegment of Fasciola hepatica Cathepsin L1 in Folding of the Catalytic Domain

M. Cappetta / I. Roth / A. Díaz / J. Tort / L. Roche
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.134

Abstract

The Nterminal propeptides of cysteine proteinases play regulatory roles in the folding and stability of their catalytic domains, as well as being potent and highly specific inhibitors of their parental mature enzymes. Cysteine proteinases play a major role in the biology of the parasitic trematode Fasciola hepatica; in particular, this organism secretes significant amounts of cathepsin L enzymes. The isolated propeptide of F. hepatica cathepsin L1 functioned as a chaperone for the mature enzyme in renaturation experiments. A double point mutation (N70I/F72I) within the GxNxFxD motif of the propeptide affected its conformation and markedly decreased its affinity for the mature enzyme. When this mutation was introduced into preprocathepsin L1 expressed in yeast, the secretion of active enzyme dropped dramatically. However, significant enzyme activity was recovered from the culture supernatants after denaturation and renaturation in the presence of native propeptide. Thus, the variant prosegment gave rise to an enzyme with altered conformation, which could be refolded to the active form with the assistance of the native propeptide.

About the article

Published Online: 2005-06-01

Published in Print: 2002-08-27


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.134.

Export Citation

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]
Mark W. Robinson, Jose F. Tort, Jonathan Lowther, Sheila M. Donnelly, Emily Wong, Weibo Xu, Colin M. Stack, Matthew Padula, Ben Herbert, and John P. Dalton
Molecular & Cellular Proteomics, 2008, Volume 7, Number 6, Page 1111
[2]
Colin M. Stack, Sheila Donnelly, Jonathan Lowther, Weibo Xu, Peter R. Collins, Linda S. Brinen, and John P. Dalton
Journal of Biological Chemistry, 2007, Volume 282, Number 22, Page 16532
[3]
Peter R. Collins, Colin M. Stack, Sandra M. O'Neill, Sean Doyle, Thecla Ryan, Gerard P. Brennan, Angela Mousley, Michael Stewart, Aaron G. Maule, John P. Dalton, and Sheila Donnelly
Journal of Biological Chemistry, 2004, Volume 279, Number 17, Page 17038
[4]
Thyago Hermylly Santana Cardoso, Ana Camila Oliveira Freitas, Bruno Silva Andrade, Aurizangela Oliveira de Sousa, André da Silva Santiago, Daniela Martins Koop, Karina Peres Gramacho, Fátima Cerqueira Alvim, Fabienne Micheli, Carlos Priminho Pirovani, and Eugene A. Permyakov
PLOS ONE, 2015, Volume 10, Number 12, Page e0144440
[5]
Jung-Mi Kang, Hye-Lim Ju, Woon-Mok Sohn, and Byoung-Kuk Na
Molecular and Biochemical Parasitology, 2013, Volume 190, Number 2, Page 92
[6]
A. Zawistowska-Deniziak, K. Wasyl, L.J. Norbury, A. Wesołowska, J. Bień, M. Grodzik, M. Wiśniewski, P. Bąska, and H. Wędrychowicz
Molecular and Biochemical Parasitology, 2013, Volume 190, Number 1, Page 27
[7]
Luis H. Gutiérrez-González, Arturo Rojo-Domínguez, Nallely E. Cabrera-González, Ruy Pérez-Montfort, and A. Jaqueline Padilla-Zúñiga
Archives of Biochemistry and Biophysics, 2006, Volume 446, Number 2, Page 151
[8]
Rosa Eréndira Fosado-Quiroz and Arturo Rojo-Domínguez
The Protein Journal, 2011, Volume 30, Number 3, Page 184

Comments (0)

Please log in or register to comment.
Log in