EC Number   |
Activating Compound |
Reference |
|---|
   1.8.3.2 | H2O2 |
high concentrations of H2O2, inducing apoptosis, cause an increase of QSOX1 mRNA and protein |
692210 |
| 1.8.3.2 | L-Cys |
fungus is not able to use L-Cys as sulfur source instead of sulfate. Presence of L-Cys induces production of an excessive amount of both intracellular and extracellular enzyme |
723985 |
| 1.8.3.2 | MgSO4 |
in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium |
723985 |
| 1.8.3.2 | more |
enzyme expression in endometrial glandular epithelium is inducible by estradiol in presence of cycloheximide, and by serum deprivation |
657645 |
| 1.8.3.2 | more |
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation |
657645 |
| 1.8.3.2 | soybean PDI family protein |
cooperative refolding of unfolded RNase A by rGmQSOX1 and all tested soybean PDI family proteins of group I and group II, but not of group III. Most effective are GmPDIL-2 and GmPDIL-1 with rGmQSOX1. These PDI family proteins contain two classic CGHC motifs in the a and a' domains, except for the group III PDI family proteins, which have nonclassic active centre CXXC motifs. The combination of rGmQSOX1 and GmPDIL-2 with an a-b-b'-a' domain structure shows the highest level of refolding activity, while the GmPDIL-2 C101A/C104A/C440A/C443A mutant, in which all of the cysteines in the two active centres are replaced with alanines, is devoid of cooperative oxidative refolding activity with rGmQSOX1. The refolding activity of rGmQSOX1 combined with the C104A/C443A mutant is 18% of that of rGmQSOX1 combined with wild-type GmPDIL-2. Analysis of the cooperation mechanism, overview |
742490 |
| 1.8.3.2 | staurosporine aglycone |
- |
692210 |
| 1.8.3.2 | Triton X-100 |
0-0.1% concentration, at most 30% activation |
393052 |
