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

Povzetek

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.

Ključne besede

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

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.01 - Izvirni znanstveni članek
Organizacija: UL FKKT - Fakulteta za kemijo in kemijsko tehnologijo
UDK: 577.15
COBISS: 1538119107 Povezava se bo odprla v novem oknu
ISSN: 1046-5928
Št. ogledov: 838
Št. prenosov: 534
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: proteoliza;oligomerni proteini;izključitvena domena;elastoliza;želatinoliza;
Vrsta dela (COBISS): Članek v reviji
Konec prepovedi (OpenAIRE): 2020-01-29
Strani: str. 21-27
Zvezek: ǂVol. ǂ157
Čas izdaje: May 2019
DOI: 10.1016/j.pep.2019.01.009
ID: 11048637