EC Number |
General Information |
Reference |
---|
3.4.21.112 | malfunction |
enzyme SKI-1 inhibition induces apoptosis of melanoma cells by a non-ATF6-dependent mechanism, overview |
732292 |
3.4.21.112 | malfunction |
in CHO cells deficient of S1P (termed SRD-12B cells) glycoprotein GP-C processing is abrogated after Lassa virus infection |
710345 |
3.4.21.112 | malfunction |
postnatal ablation of site-1 protease results in chondrodysplasia and rapid growth plate disruption due to intracellular Col II entrapment concomitant with loss of chondrocyte hypertrophy. S1P ablation at E10.5 results in a complete loss of endochondral bone formation along with the presence of an enhanced cortical bone formation |
717840 |
3.4.21.112 | malfunction |
soluble enzyme is unable to process arenavirus glycoproteinss at the cell surface |
732412 |
3.4.21.112 | more |
9 amino acid residues at the cleavage site (P1-P8) and P1' are necessary and sufficient to define the subcellular location of processing and to determine to what extent processing of a substrate depends on SKI-1/S1P maturation |
732162 |
3.4.21.112 | more |
modeling of the SKI-1/S1P catalytic pocket identifies Y285 as a residue that potentially interacts with arenavirus envelope glycoprotein precursor residue Y253. The the catalytic triad is formed by residues D218, H249, and S414 |
732421 |
3.4.21.112 | more |
the transmembrane anchorage and the cytoplasmic domain of SKI-1/S1P are dispensable for arenavirus glycoprotein processing |
732412 |
3.4.21.112 | physiological function |
a crucial step in the life cycle of arenaviruses is the biosynthesis of the mature fusion-active viral envelope glycoprotein that is essential for virus-host cell attachment and entry. The maturation of the arenavirus envelope glycoprotein precursor critically depends on proteolytic processing by the cellular proprotein convertase subtilisin kexin isozyme-1/site-1 protease |
732412 |
3.4.21.112 | physiological function |
inhibition of S1P enzymatic activity in human hepatoma Huh-7.5.1 cells results in a robust reduction of the numbers of lipid droplets and lipid droplet-positive areas and effectively inhibits infection by dengue virsu DENV. Pre-treatment of Huh-7.5.1 cells with PF-429242 results in a dose-dependent inhibition of DENV and an about 3-log decrease in DENV-2 titer with 20 microM of PF-429242. Post-treatment of DENV-2 infected Huh-7.5.1 cells with PF-429242 does not affect viral RNA abundance, but it does compromise the assembly and/or release of infectious virus particles. PF-429242 antiviral activity is reversed by exogenous oleic acid |
755140 |
3.4.21.112 | physiological function |
inhibition of site-1 protease leads to a profound reduction in plasmablast number linked to induction of autophagy. Plasmablasts generated in the presence of site-1 protease inhibitor segregate into CD38high and CD38low populations, the latter characterized by a marked reduction in the capacity to secrete IgG. Site-1 protease inhibition is accompanied by a distinctive change in gene expression associated with amino acid, steroid and fatty acid synthesis pathways |
755495 |