izpis_h1_title_alt

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

.pdfPDF - Presentation file, Download (1,05 MB)
MD5: CD3D123F939AD4F2A0D00BB0817FC01A
URLURL - Source URL, Visit https://www.sciencedirect.com/science/article/pii/S1046592819300105 This link opens in a new window

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.

Language:English
Keywords:proteolysis, oligomeric proteins, exclusion domain, elastolysis, gelatinolysis
Work type:Article
Typology:1.01 - Original Scientific Article
Organization:FKKT - Faculty of Chemistry and Chemical Technology
Publication status:Published
Publication version:Author Accepted Manuscript
Year:2019
Number of pages:Str. 21-27
Numbering:Vol. 157
PID:20.500.12556/RUL-106687 This link opens in a new window
UDC:577.15
ISSN on article:1046-5928
DOI:10.1016/j.pep.2019.01.009 This link opens in a new window
COBISS.SI-ID:1538119107 This link opens in a new window
Publication date in RUL:12.03.2019
Views:1271
Downloads:749
Metadata:XML RDF-CHPDL DC-XML DC-RDF
:
Copy citation
Share:Bookmark and Share

Record is a part of a journal

Title:Protein expression and purification
Shortened title:Protein expr. purif.
Publisher:Elsevier, Academic Press
ISSN:1046-5928
COBISS.SI-ID:2627623 This link opens in a new window

Licences

License:CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.
Licensing start date:12.03.2019

Secondary language

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

Projects

Funder:ARRS - Slovenian Research Agency
Project number:P1-0140
Name:Proteoliza in njena regulacija

Similar documents

Similar works from RUL:
Similar works from other Slovenian collections:

Back