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Literature summary extracted from

  • Thorpe, C.; Hoober, K.L.; Raje, S.; Glynn, N.M.; Burnside, J.; Turi, G.K.; Coppock, D.L.
    Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes (2002), Arch. Biochem. Biophys., 405, 1-12.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.3.2 additional information enzyme expression in endometrial glandular epithelium is inducible by estradiol in presence of cycloheximide, and by serum deprivation Cavia porcellus
1.8.3.2 additional information enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.2 DNA and amino acid sequence determination and analysis, gene structure Gallus gallus
1.8.3.2 DNA and amino acid sequence determination and analysis, gene structure Cavia porcellus
1.8.3.2 DNA and amino acid sequence determination and analysis, gene structure Trypanosoma brucei
1.8.3.2 DNA and amino acid sequence determination and analysis, gene structure Rattus norvegicus
1.8.3.2 genes ERV1 and ERV2, DNA and amino acid sequence determination and analysis, gene structure, phylogenetic analysis Saccharomyces cerevisiae
1.8.3.2 genes QSCN6 or QSOX1, and QSOX2, DNA and amino acid sequence determination and analysis, QSCN6 or QSOX1 is located on chromosome 1q25.2, QSOX2 on chromosome 9q34, gene structure Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.3.2 Erv2p, X-ray diffraction structure determination and analysis Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.2 additional information
-
 additional information the activity with small thiols is dominated by the Km value Gallus gallus
1.8.3.2 additional information
-
 additional information the activity with small thiols is dominated by the Km value Rattus norvegicus
1.8.3.2 0.0046
-
 O2
-
 Gallus gallus
1.8.3.2 0.02
-
 glutathione
-
 Gallus gallus
1.8.3.2 0.7
-
 dithiothreitol
-
 Rattus norvegicus
1.8.3.2 4.4
-
 glutathione
-
 Rattus norvegicus
1.8.3.2 6.9
-
 DTT Evr2p Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.2 apocrine cell
-
 Homo sapiens
-
-
1.8.3.2 cytoplasm
-
 Saccharomyces cerevisiae 5737
-
1.8.3.2 endoplasmic reticulum
-
 Saccharomyces cerevisiae 5783
-
1.8.3.2 endoplasmic reticulum
-
 Homo sapiens 5783
-
1.8.3.2 extracellular
-
 Saccharomyces cerevisiae
-
-
1.8.3.2 extracellular egg white Gallus gallus
-
-
1.8.3.2 extracellular secretion by fungal mycelium Aspergillus niger
-
-
1.8.3.2 extracellular seminal vesicles Homo sapiens
-
-
1.8.3.2 Golgi apparatus
-
 Homo sapiens 5794
-
1.8.3.2 mitochondrial intermembrane space high concentration of Evr1p Saccharomyces cerevisiae 5758
-
1.8.3.2 nucleus
-
 Saccharomyces cerevisiae 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.2 Iron enzyme contains a FeS center Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.3.2 53000
-
 2 * 53000 Aspergillus niger
1.8.3.2 65000
-
 1 * 65000, about Rattus norvegicus
1.8.3.2 90000
-
 2 * 90000, about Gallus gallus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.2 insulin A and B chains + O2 Gallus gallus
-
 disulfide of insulin A and B chains + H2O2
-
 ?
1.8.3.2 lysozyme + O2 Gallus gallus
-
 lysozyme disulfide + H2O2
-
 ?
1.8.3.2 additional information Saccharomyces cerevisiae Evr1p is involved in cellular iron homeostasis, physiological role of the ERV1/ALR family enzymes, overview ?
-
 ?
1.8.3.2 additional information Gallus gallus preferred substrates are protein or peptide sulfhydryl groups, even of denatured cytoplasmic proteins, low molecular weight thiols, such as cysteine or glutathione, are poorer substrates ?
-
 ?
1.8.3.2 ovalbumin + O2 Gallus gallus
-
 ovalbumin disulfide + H2O2
-
 ?
1.8.3.2 R-SH + O2 Cavia porcellus
-
 R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 Saccharomyces cerevisiae
-
 R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 Aspergillus niger
-
 R-S-S-R + H2O2
-
 ir
1.8.3.2 R-SH + O2 Trypanosoma brucei
-
 R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 Gallus gallus enzyme plays a significant role in oxidative folding of a large variety of proteins R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 Rattus norvegicus enzyme plays a significant role in oxidative folding of a large variety of proteins R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 Homo sapiens enzyme plays a significant role in oxidative folding of a large variety of proteins R-S-S-R + H2O2
-
 ?
1.8.3.2 riboflavin-binding protein + O2 Gallus gallus
-
 riboflavin-binding protein disulfide + H2O2
-
 ?
1.8.3.2 RNase A + O2 Gallus gallus
-
 RNase A disulfide + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Aspergillus niger
-
-
-
1.8.3.2 Cavia porcellus
-
-
-
1.8.3.2 Gallus gallus
-
-
-
1.8.3.2 Homo sapiens O00391 gene QSOX1
-
1.8.3.2 Rattus norvegicus Q6IUU3 gene QSOX1
-
1.8.3.2 Saccharomyces cerevisiae
-
 2 isozymes Evr1p and Evr2p
-
1.8.3.2 Trypanosoma brucei
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.8.3.2 glycoprotein highly glycosylated Gallus gallus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.3.2 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 mechanistic scheme Gallus gallus
a
1.8.3.2 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 the CXXC motif in the active site sequence of Erv2p is catalytically essential, reaction mechanism involving reactive cysteine residues C121 and C124 of the A subunit, and C176 and C178 of the B subunit Saccharomyces cerevisiae
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.2 egg white
-
 Gallus gallus
-
1.8.3.2 endometrium glandular epithelial cells Cavia porcellus
-
1.8.3.2 epididymis high content Rattus norvegicus
-
1.8.3.2 epithelium endometrial glandular Cavia porcellus
-
1.8.3.2 fibroblast high expression level of QSOX1 Homo sapiens
-
1.8.3.2 additional information wide tissue distribution Gallus gallus
-
1.8.3.2 additional information tissue expression and distribution Rattus norvegicus
-
1.8.3.2 additional information tissue expression and distribution, high enzyme concentration in cell types associated with heavy secretory loads Homo sapiens
-
1.8.3.2 mycelium secretion of enzyme Aspergillus niger
-
1.8.3.2 oviduct secretory tissue Gallus gallus
-
1.8.3.2 seminal vesicle high content Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 dithiothreitol + O2
-
 Gallus gallus dithiothreitol disulfide + H2O2
-
 ?
1.8.3.2 dithiothreitol + O2
-
 Rattus norvegicus dithiothreitol disulfide + H2O2
-
 r
1.8.3.2 dithiothreitol + O2 Evr2p, not Evr1p Saccharomyces cerevisiae dithiothreitol disulfide + H2O2
-
 ?
1.8.3.2 glutathione + O2
-
 Gallus gallus glutathione disulfide + H2O2
-
 ?
1.8.3.2 glutathione + O2
-
 Rattus norvegicus glutathione disulfide + H2O2
-
 ?
1.8.3.2 glutathione + O2 best small thiol substrate Aspergillus niger glutathione disulfide + H2O2
-
 ?
1.8.3.2 glutathione + O2 Evr2p, not Evr1p Saccharomyces cerevisiae glutathione disulfide + H2O2
-
 ?
1.8.3.2 insulin A and B chains + O2
-
 Gallus gallus disulfide of insulin A and B chains + H2O2
-
 ?
1.8.3.2 lysozyme + O2
-
 Gallus gallus lysozyme disulfide + H2O2
-
 ?
1.8.3.2 lysozyme + O2 Evr1p Saccharomyces cerevisiae lysozyme disulfide + H2O2
-
 ?
1.8.3.2 additional information Evr1p is involved in cellular iron homeostasis, physiological role of the ERV1/ALR family enzymes, overview Saccharomyces cerevisiae ?
-
 ?
1.8.3.2 additional information preferred substrates are protein or peptide sulfhydryl groups, even of denatured cytoplasmic proteins, low molecular weight thiols, such as cysteine or glutathione, are poorer substrates Gallus gallus ?
-
 ?
1.8.3.2 additional information low activity with reduced proteins Aspergillus niger ?
-
 ?
1.8.3.2 ovalbumin + O2
-
 Gallus gallus ovalbumin disulfide + H2O2
-
 ?
1.8.3.2 R-SH + O2
-
 Cavia porcellus R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2
-
 Saccharomyces cerevisiae R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2
-
 Aspergillus niger R-S-S-R + H2O2
-
 ir
1.8.3.2 R-SH + O2
-
 Trypanosoma brucei R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2
-
 Rattus norvegicus R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2
-
 Homo sapiens R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 enzyme plays a significant role in oxidative folding of a large variety of proteins Gallus gallus R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 enzyme plays a significant role in oxidative folding of a large variety of proteins Rattus norvegicus R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 enzyme plays a significant role in oxidative folding of a large variety of proteins Homo sapiens R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 best substrates are cysteine residues in reduced proteins Gallus gallus R-S-S-R + H2O2
-
 ?
1.8.3.2 riboflavin-binding protein + O2
-
 Gallus gallus riboflavin-binding protein disulfide + H2O2
-
 ?
1.8.3.2 RNase A + O2
-
 Gallus gallus RNase A disulfide + H2O2
-
 ?
1.8.3.2 RNase A + O2
-
 Rattus norvegicus RNase A disulfide + H2O2
-
 ?
1.8.3.2 RNase A + O2 low activity Aspergillus niger RNase A disulfide + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.3.2 dimer
-
 Saccharomyces cerevisiae
1.8.3.2 dimer 2 * 53000 Aspergillus niger
1.8.3.2 dimer 2 * 90000, about Gallus gallus
1.8.3.2 monomer 1 * 65000, about Rattus norvegicus
1.8.3.2 More structure Gallus gallus
1.8.3.2 More structure, active site structure containinbg a CXXC motif Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 Erv1p
-
 Saccharomyces cerevisiae
1.8.3.2 ERv2p
-
 Saccharomyces cerevisiae
1.8.3.2 More enzyme belongs to the ERV1/ALR family Saccharomyces cerevisiae
1.8.3.2 More enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family Gallus gallus
1.8.3.2 More enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family Cavia porcellus
1.8.3.2 More enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family Trypanosoma brucei
1.8.3.2 More enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family Rattus norvegicus
1.8.3.2 More enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family Homo sapiens
1.8.3.2 QSCN6
-
 Homo sapiens
1.8.3.2 QSOX
-
 Gallus gallus
1.8.3.2 QSOX
-
 Cavia porcellus
1.8.3.2 QSOX
-
 Trypanosoma brucei
1.8.3.2 QSOX
-
 Rattus norvegicus
1.8.3.2 QSOx1
-
 Homo sapiens
1.8.3.2 QSOX2
-
 Homo sapiens
1.8.3.2 Quiescin Q6
-
 Homo sapiens
1.8.3.2 Quiescin-sulfhydryl oxidase
-
 Gallus gallus
1.8.3.2 Quiescin-sulfhydryl oxidase
-
 Cavia porcellus
1.8.3.2 Quiescin-sulfhydryl oxidase
-
 Trypanosoma brucei
1.8.3.2 Quiescin-sulfhydryl oxidase
-
 Rattus norvegicus
1.8.3.2 Quiescin-sulfhydryl oxidase
-
 Homo sapiens
1.8.3.2 sulfhydryl oxidase
-
 Gallus gallus
1.8.3.2 sulfhydryl oxidase
-
 Cavia porcellus
1.8.3.2 sulfhydryl oxidase
-
 Aspergillus niger
1.8.3.2 sulfhydryl oxidase
-
 Trypanosoma brucei
1.8.3.2 sulfhydryl oxidase
-
 Rattus norvegicus
1.8.3.2 sulfhydryl oxidase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.3.2 additional information
-
 additional information
-
 Gallus gallus
1.8.3.2 0.002
-
 RNAse A thiol per second Aspergillus niger
1.8.3.2 3.5
-
 DTT 3°C Gallus gallus
1.8.3.2 4
-
 DTT Evr2p Saccharomyces cerevisiae
1.8.3.2 20
-
 DTT 25°C Gallus gallus
1.8.3.2 66.67
-
 glutathione
-
 Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 FAD
-
 Aspergillus niger
1.8.3.2 FAD small FAD-binding domain Cavia porcellus
1.8.3.2 FAD small FAD-binding domain Trypanosoma brucei
1.8.3.2 FAD small FAD-binding domain Rattus norvegicus
1.8.3.2 FAD small FAD-binding domain Homo sapiens
1.8.3.2 FAD small FAD-binding domain, 1 molecule per subunit Gallus gallus
1.8.3.2 additional information enzyme contains a thioredoxin and a ERV1 domain Trypanosoma brucei
1.8.3.2 additional information enzyme contains a thioredoxin and an ERV1 domain Saccharomyces cerevisiae
1.8.3.2 additional information enzyme contains a thioredoxin domain Cavia porcellus
1.8.3.2 additional information enzyme contains a thioredoxin domain Rattus norvegicus
1.8.3.2 additional information enzyme contains a thioredoxin domain Homo sapiens
1.8.3.2 additional information enzyme contains a thioredoxin domain, 1 redox-active disulfide per subunit Gallus gallus
1.8.3.2 additional information redox-active disulfide involved in catalysis Aspergillus niger