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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

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IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

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Volume 383, Issue 7-8


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


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, Volume 383, Issue 7-8, Pages 1215–1221, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.134.

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