Mateja Presečnik (Author), Brigita Lenarčič (Author), Marko Novinec (Author)

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.

Keywords

proteoliza;oligomerni proteini;izključitvena domena;elastoliza;želatinoliza;proteolysis;oligomeric proteins;exclusion domain;elastolysis;gelatinolysis;

Data

Language: English
Year of publishing:
Typology: 1.01 - Original Scientific Article
Organization: UL FKKT - Faculty of Chemistry and Chemical Technology
UDC: 577.15
COBISS: 1538119107 Link will open in a new window
ISSN: 1046-5928
Views: 838
Downloads: 534
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Other data

Secondary language: Slovenian
Secondary keywords: proteoliza;oligomerni proteini;izključitvena domena;elastoliza;želatinoliza;
Type (COBISS): Article
Embargo end date (OpenAIRE): 2020-01-29
Pages: str. 21-27
Issue: ǂVol. ǂ157
Chronology: May 2019
DOI: 10.1016/j.pep.2019.01.009
ID: 11048637