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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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Volume 382, Issue 5


Cathepsins X and B Display Distinct Activity Profiles That Can Be Exploited for Inhibitor Design

R. Ménard / C. Therrien / P. Lachance / T. Sulea / H. Qi / A. Alvarez-Hernandez / W.R. Roush .
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2001.102


The carboxypeptidase and endopeptidase activities of cathepsins X and B, as well as their inhibition by E 64 derivatives, have been investigated in detail and compared. The results clearly demonstrate that cathepsins X and B do not share similar activity profiles against substrates and inhibitors. Using quenched fluorogenic substrates, we show that cathepsin X preferentially cleaves substrates through a monopeptidyl carboxypeptidase pathway, while cathepsin B displays a preference for the dipeptidyl pathway. The preference for one or the other pathway is about the same for both enzymes, i. e. approximately 2 orders of magnitude. Cleavage of a Cterminal dipeptide of a substrate by cathepsin X can be observed under conditions that preclude efficient monopeptidyl carboxypeptidase activity. In addition, an inhibitor designed to exploit the unique structural features responsible for the carboxypeptidase activity of cathepsin X has been synthesized and tested against cathepsins X, B and L. Although of moderate potency, this E-64 derivative is the first reported example of a cathepsin Xspecific inhibitor. By comparison, CA074 was found to inactivate cathepsin B at least 34000-fold more efficiently than cathepsin X.

About the article

Published Online: 2005-06-01

Published in Print: 2001-05-05

Citation Information: Biological Chemistry, Volume 382, Issue 5, Pages 839–845, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2001.102.

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