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Literature summary for 5.3.4.1 extracted from
- Enzymatic catalysis of disulfide formation (1994), Protein Expr. Purif., 5, 1-13.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | useful in facilitating the in vitro folding of proteins | Bacteria |
| synthesis | useful in facilitating the in vitro folding of proteins | eukaryota |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C35S | mutagenesis of Cys35 or Cys379 to a Ser causes loss of activity | Rattus norvegicus |
| C379S | mutagenesis of Cys35 or Cys379 to a Ser causes loss of activity | Rattus norvegicus |
| C55S/C379S | The double active site mutant Cys55Ser, Cys379Ser is not capable of catalyzing protein folding | Rattus norvegicus |
| G36A | Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity | Rattus norvegicus |
| H37P | Mutagenesis of His37 to a Pro causes almost complete loss of activity | Rattus norvegicus |
| L39R | Mutagenesis of Lys39 to an Arg results in only a modest loss of activity | Rattus norvegicus |
| W34S | Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Saccharomyces cerevisiae | 5783 | - |
| endoplasmic reticulum | lumen | eukaryota | 5783 | - |
| endoplasmic reticulum | lumen | Rattus norvegicus | 5783 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | eukaryota | the enzyme acts as a thyroid-hormone binding protein | ? | - |
? |  |
| Proteins | Bacteria | - |
? | - |
? | |
| Proteins | Rattus norvegicus | - |
? | - |
? | |
| Proteins | eukaryota | facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacteria | - |
- |
- |
| eukaryota | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| catalyses the rearrangement of -S-S- bonds in proteins | mechanism | eukaryota | |
| catalyses the rearrangement of -S-S- bonds in proteins | mechanism | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme acts as a thyroid-hormone binding protein | eukaryota | ? | - |
? | |
| Proteins | native, reduced or with wrong disulfide bonds | Bacteria | Proteins | with correct disulfide bonds | ? | |
| Proteins | native, reduced or with wrong disulfide bonds | eukaryota | Proteins | with correct disulfide bonds | ? | |
| Proteins | native, reduced or with wrong disulfide bonds | Rattus norvegicus | Proteins | with correct disulfide bonds | ? | |
| Proteins | native, reduced or with wrong disulfide bonds | Saccharomyces cerevisiae | Proteins | with correct disulfide bonds | ? | |
| Proteins | - |
Bacteria | ? | - |
? | |
| Proteins | - |
Rattus norvegicus | ? | - |
? | |
| Proteins | facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins | eukaryota | ? | - |
? | |
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