Application | Comment | Organism |
---|---|---|
medicine | te enzyme might be useful in therapeutic strategies for treating prion diseases | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | binding kinetics of immobilized QSOX to various PrP prion proteins | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | quiescin-sulfhydryl oxidase (QSOX) catalyzes the facile direct introduction of disulfide bonds into unfolded, reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains, the affinity of QSOX for monomer is significantly lower than that for octamer. QSOX exhibits much lower affinity for N-terminally truncated murine prion protein (PrP89-230) than for the full-length murine prion protein (PrP23-231), suggesting that the N-terminal region of prion protein is critical for the interaction of prion protein with QSOX | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Homo sapiens | - |
ScN2a cell | - |
Homo sapiens | - |
seminal vesicle | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | quiescin-sulfhydryl oxidase (QSOX) catalyzes the facile direct introduction of disulfide bonds into unfolded, reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains, the affinity of QSOX for monomer is significantly lower than that for octamer. QSOX exhibits much lower affinity for N-terminally truncated murine prion protein (PrP89-230) than for the full-length murine prion protein (PrP23-231), suggesting that the N-terminal region of prion protein is critical for the interaction of prion protein with QSOX | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
QSOX | - |
Homo sapiens |
Quiescin-sulfhydryl oxidase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | enzyme QSOX is an evolutionarily conserved protein present in organisms ranging from the smallest free-living eukaryotes to humans | Homo sapiens |
physiological function | quiescin-sulfhydryl oxidase (QSOX) plays a role in protein folding by introducing disulfides into unfolded reduced proteins. Quiescin-sulfhydryl oxidase inhibits formation of prions, infectious glycoproteins that cause a group of fatal transmissible diseases in animals and humans, in vitro. QSOX inhibits human prion propagation in protein misfolding cyclic amplification reactions and murine prion propagation in scrapie-infected neuroblastoma cells. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains | Homo sapiens |