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 |
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 |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.8.3.2 | Erv2p, X-ray diffraction structure determination and analysis | Saccharomyces cerevisiae |
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 |
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 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.8.3.2 | Iron | enzyme contains a FeS center | Saccharomyces cerevisiae |
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 |
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 | - |
? |
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 | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.8.3.2 | glycoprotein | highly glycosylated | Gallus gallus |
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 | |
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 |
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 | - |
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 | - |
? |
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 |
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 |
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 |
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 |