The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease.
Elastolysis
Exclusion domain
Gelatinolysis
Oligomeric proteins
Proteolysis
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
07
01
2019
accepted:
25
01
2019
pubmed:
1
2
2019
medline:
10
4
2020
entrez:
1
2
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 30703555
pii: S1046-5928(19)30010-5
doi: 10.1016/j.pep.2019.01.009
pii:
doi:
Substances chimiques
Recombinant Proteins
0
Gelatin
9000-70-8
Collagen
9007-34-5
Elastin
9007-58-3
Cathepsin C
EC 3.4.14.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
21-27Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.