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Literature summary for 1.8.3.2 extracted from
- Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation (2003), Biochemistry, 42, 4560-4568.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.14 | - |
DTT | native enzyme, pH 7.5 | Gallus gallus |  |
| 12.5 | - |
DTT | 60 kDa enzyme fragment, pH 7.5 | Gallus gallus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 100000 | - |
x * 100000, native enzyme, SDS-PAGE | Gallus gallus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| R-SH + O2 | Gallus gallus | oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide | R-S-S-R + H2O2 | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | heavy glycosylation of the 60-kDa-enzyme fragment | Gallus gallus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| intact enzyme and proteolytically cleaved enzyme in 30 kDa and 60 kDa fragments | Gallus gallus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| egg white | - |
Gallus gallus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dithiothreitol + O2 | intact enzyme and 60-kDa-enzyme fragment | Gallus gallus | dithiothreitol disulfide + H2O2 | - |
ir | |
| additional information | a 30 kDa enzyme fragment shows no catalytic activity of its own | Gallus gallus | ? | - |
? | |
| R-SH + O2 | oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide | Gallus gallus | R-S-S-R + H2O2 | - |
ir | |
| RNase A + O2 | intact enzyme, but not 60-kDa-enzyme fragment | Gallus gallus | RNase A disulfide + H2O2 | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 100000, native enzyme, SDS-PAGE | Gallus gallus |
| More | 2 enzyme fragments by partial proteolysis: a 30 kDa nonglycosylated monomeric fragment containing a thioredoxin domain with a CXXC motif, and a 60 kDa glycosylated dimeric fragment with bound FAD and catalytic activity, the latter different from intact enzyme activity | Gallus gallus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family | Gallus gallus |
| QSOX | - |
Gallus gallus |
| sulfhydryl oxidase | - |
Gallus gallus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1013 | - |
DTT | native enzyme, pH 7.5 | Gallus gallus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Gallus gallus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | required for activity, binding domain is located on the 60-kDa-enzyme fragment, electron-transfer mechanism in the native enzyme and the 60 kDA enzyme fragment | Gallus gallus | |
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