The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease
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Updated: Jan 30, 2026

A Simple and Efficient Protocol for the Catalytic Insertion Polymerization of Functional Norbornenes
Published on: February 27, 2017
Mateja Rebernik1, Brigita Lenarčič2, Marko Novinec1
1Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical technology, University of Ljubljana, Večna pot 113, 1000, Ljubljana, Slovenia.
Abstract:
Cathepsin C is a tetrameric lysosomal protease that acts as a dipeptidyl-peptidase due to the presence of the exclusion domain that is unique among papain-like cysteine proteases. Here we describe a recombinant form of cathepsin C lacking its exclusion domain (CatCΔEx) produced in a bacterial expression system (E. coli). CatCΔEx is a monomer with endoprotease activity and affinity for hydrophobic residues such as Phe, Leu or Pro, but not Val, in the P2 position. As opposed to cathepsin C, it does not require chloride ions for its activity. Despite lower turnover rates of hydrolysis of synthetic substrates, CatCΔEx has elastolytic and gelatinolytic activity comparable to other cysteine cathepsins.
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