EC Number   |
Activating Compound |
Reference |
|---|
   3.4.21.75 | Ca2+ |
parasite expresses a Ca2+ dependent, furin-like protease activity |
680137 |
| 3.4.21.75 | heparin |
optimizies furin processing of substrates containing multibasic residues at strategic P-positions within the cleavage site. Incubation of Fujian-like peptides with heparin results in ca. 2- to 3fold enhancement of processing. Heparin at a concentration of 0.02 mM dramatically enhances processing of the basic highly pathogenic Queretaro H5N2 peptide, albeit at neutral pH. It has no effect on processing of low pathogenic Mexico H5N2 peptide |
681510 |
| 3.4.21.75 | more |
expression of furin in irradiated Colo-16 cells remains constant for 48 h following exposure of the cells to either low dose UVA and/or UVB radiation, and high-dose UVA radiation. In cells irradiated with high-dose UVB radiation, significant increase in furin expression commencing at 12 h, which peaks at 24 h (5fold). Correlation between expression of pp38 and furin in Colo-16 cells, but not HaCaT cells, following UV exposure |
700627 |
| 3.4.21.75 | more |
furin induced by interleukin 12 |
678910 |
| 3.4.21.75 | more |
furin is up-regulated by iron deficiency and hypoxia in association with the stabilization of HIF-1alpha |
678922 |
| 3.4.21.75 | more |
heparin-peptide interaction may better expose site1, and hence allow more effective furin cleavage. Extended sequences require heparin for optimal processing by furin |
679871 |
| 3.4.21.75 | more |
His69 controls the pH-sensitive furin propeptide cleavage and enzyme activation in vitro. Protonated His69 disrupts the propeptide to expose the internal cleavage site and increases the efficiency of cleavage at Arg75 to yield the active enzyme |
680654 |
| 3.4.21.75 | more |
in the presence of trifluoroethanol, the N-terminal half of the prodomain is better structured and more compactly folded than the C-terminal half of the prodomain. N-terminal residues 1-46 of the prodomain in 50% trifluoroethanol populates backbone conformations containing a short helix, a beta-strand and a helix-loop-helix supersecondary structure with elements of tertiary interactions. The intervening segment (residues 47-65) is predominately unstructured with a long and highly flexible region surrounding the protease activation loop followed by a partially helical segment in the C-terminal end. A peptide fragment derived from residues Pro16-Arg49 can form the helix-loop-helix structure in aqueous solution in the absence of trifluoroethanol |
678743 |
| 3.4.21.75 | more |
L-Sox5 and Sox-6 act as negative regulators of Sox9-induced furin expression |
677460 |
| 3.4.21.75 | more |
relationship between Sox-9 dependent expression of furin and the maturation/bioactivation of substrates involved in chondrogenesis. Peak expression of both furin mRNA and furin parathyroid hormone-related peptide maturation in ATDC5 cells during chondrocyte nodule formation stage |
677460 |
