Literature summary for 1.8.3.2 extracted from

Zhan, Y.A.; Abskharon, R.; Li, Y.; Yuan, J.; Zeng, L.; Dang, J.; Martinez, M.C.; Wang, Z.; Mikol, J.; Lehmann, S.; Bu, S.; Steyaert, J.; Cui, L.; Petersen, R.B.; Kong, Q.; Wang, G.X.; Wohlkonig, A.; Zou, W.Q.
Quiescin-sulfhydryl oxidase inhibits prion formation in vitro (2016), Aging, 8, 3419-3429 .

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Application

Application	Comment	Organism
medicine	te enzyme might be useful in therapeutic strategies for treating prion diseases	Homo sapiens

KM Value [mM]

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Homo sapiens	-
ScN2a cell	-	Homo sapiens	-
seminal vesicle	-	Homo sapiens	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
QSOX	-	Homo sapiens
Quiescin-sulfhydryl oxidase	-	Homo sapiens

General Information

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

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Release 2023.1 (January 2023)