20.500.12556/RUL-106687 The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease 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. proteolysis oligomeric proteins exclusion domain elastolysis gelatinolysis proteoliza oligomerni proteini izključitvena domena elastoliza želatinoliza true false true Angleški jezik Slovenski jezik Članek v reviji 2019-03-12 12:32:20 2019-03-12 12:32:21 2022-08-19 03:46:41 0000-00-00 00:00:00 2019 0 0 Str. 21-27 Vol. 157 2019 0000-00-00 PostprintKoncna Objavljeno NiDoloceno 0000-00-00 0000-00-00 0000-00-00 2020-01-29 577.15 1046-5928 10.1016/j.pep.2019.01.009 1538119107 2627623 RAZ_Rebernik_Mateja_i2019.pdf RAZ_Rebernik_Mateja_i2019.pdf 1 CD3D123F939AD4F2A0D00BB0817FC01A affe57829e91e6a669db48bf3b92f0d9c854ff5d03d1b079ebcaeafdf9fa138a 5d6a7c72-a1b6-11eb-a523-00155dcfd717 https://repozitorij.uni-lj.si/Dokument.php?lang=slv&id=117490 https://www.sciencedirect.com/science/article/pii/S1046592819300105 1 https://repozitorij.uni-lj.si/Dokument.php?lang=slv&id=117470 Fakulteta za kemijo in kemijsko tehnologijo 0 0 0