The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease
Rebernik, Mateja (Author), Lenarčič, Brigita (Author), Novinec, Marko (Author)

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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:proteolysis, oligomeric proteins, exclusion domain, elastolysis, gelatinolysis
Tipology:1.01 - Original Scientific Article
Organization:FKKT - Faculty of Chemistry and Chemical Technology
Number of pages:str. 21-27
Numbering:Vol. 157
ISSN on article:1046-5928
DOI:10.1016/j.pep.2019.01.009 Link is opened in a new window
COBISS.SI-ID:1538119107 Link is opened in a new window
License:CC BY-NC-ND 4.0
This work is available under this license: Creative Commons Attribution Non-Commercial No Derivatives 4.0 International
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Record is a part of a journal

Title:Protein expression and purification
Shortened title:Protein expr. purif.
COBISS.SI-ID:2627623 New window

Document is financed by a project

Funder:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Funding Programme:Ciljni raziskovalni programi
Project no.:P1-0140
Name:Proteoliza in njena regulacija
Project ID:info:eu-repo/grantAgreement/ARRS/Ciljni%20raziskovalni%20programi/P1-0140

Secondary language

Keywords:proteoliza, oligomerni proteini, izključitvena domena, elastoliza, želatinoliza

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