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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year

IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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Volume 384, Issue 6


Family C1 Cysteine Proteases: Biological Diversity or Redundancy?

D. K. Nägler / R. Ménard
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2003.094


Recent progress in the identification and partial characterization of novel genes encoding cysteine proteases of the papain family has considerably increased our knowledge of this family of enzymes. Kinetic data available to date for this large family indicate relatively broad, overlapping specificities for most enzymes, thus inspiring a growing conviction that they may exhibit functional redundancy. This is also supported in part by phenotypes of cathepsin knockout mice and suggests that several proteases can substitute for each other to degrade or process a given substrate. On the other hand, specific functions of one particular protease have also been documented. In addition, differences in cellular distribution and intracellular localization may contribute to defining specific functional roles for some of these proteases.

About the article

Published Online: 2005-06-01

Published in Print: 2003-06-16

Citation Information: Biological Chemistry, Volume 384, Issue 6, Pages 837–843, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2003.094.

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