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Literature summary extracted from
- Protein disulfide isomerase: the structure of oxidative folding (2006), Trends Biochem. Sci., 31, 455-464.
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 5.3.4.1 | chloroplast | - |
Chlamydomonas reinhardtii | 9507 | - |
| 5.3.4.1 | chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| 5.3.4.1 | endoplasmic reticulum | - |
Chlamydomonas reinhardtii | 5783 | - |
| 5.3.4.1 | endoplasmic reticulum | - |
Arabidopsis thaliana | 5783 | - |
| 5.3.4.1 | endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
| 5.3.4.1 | endoplasmic reticulum | - |
Saccharomyces cerevisiae | 5783 | - |
| 5.3.4.1 | membrane | - |
Escherichia coli | 16020 | - |
| 5.3.4.1 | periplasm | - |
Escherichia coli | - |
- |
| 5.3.4.1 | thylakoid membrane | - |
Arabidopsis thaliana | 42651 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.4.1 | additional information | Escherichia coli | PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview | ? | - |
? |  |
| 5.3.4.1 | additional information | Chlamydomonas reinhardtii | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | ? | - |
? | |
| 5.3.4.1 | additional information | Arabidopsis thaliana | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | ? | - |
? | |
| 5.3.4.1 | additional information | Homo sapiens | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | ? | - |
? | |
| 5.3.4.1 | additional information | Saccharomyces cerevisiae | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | Arabidopsis thaliana | - |
- |
- |
| 5.3.4.1 | Chlamydomonas reinhardtii | - |
- |
- |
| 5.3.4.1 | Escherichia coli | - |
- |
- |
| 5.3.4.1 | Homo sapiens | P07237 | - |
- |
| 5.3.4.1 | Saccharomyces cerevisiae | P17967 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.3.4.1 | catalyses the rearrangement of -S-S- bonds in proteins | substrate binding and catalytic mechanism | Chlamydomonas reinhardtii | |
| 5.3.4.1 | catalyses the rearrangement of -S-S- bonds in proteins | substrate binding and catalytic mechanism | Escherichia coli | |
| 5.3.4.1 | catalyses the rearrangement of -S-S- bonds in proteins | substrate binding and catalytic mechanism | Arabidopsis thaliana | |
| 5.3.4.1 | catalyses the rearrangement of -S-S- bonds in proteins | substrate binding and catalytic mechanism | Homo sapiens | |
| 5.3.4.1 | catalyses the rearrangement of -S-S- bonds in proteins | substrate binding and catalytic mechanism | Saccharomyces cerevisiae |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | pancreas | PDIp | Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.4.1 | additional information | PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview | Escherichia coli | ? | - |
? | |
| 5.3.4.1 | additional information | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | Chlamydomonas reinhardtii | ? | - |
? | |
| 5.3.4.1 | additional information | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | Arabidopsis thaliana | ? | - |
? | |
| 5.3.4.1 | additional information | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | Homo sapiens | ? | - |
? | |
| 5.3.4.1 | additional information | structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview | Saccharomyces cerevisiae | ? | - |
? | |
| 5.3.4.1 | additional information | PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview | Escherichia coli | ? | - |
? | |
| 5.3.4.1 | additional information | PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview | Chlamydomonas reinhardtii | ? | - |
? | |
| 5.3.4.1 | additional information | PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview | Arabidopsis thaliana | ? | - |
? | |
| 5.3.4.1 | additional information | PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview | Homo sapiens | ? | - |
? | |
| 5.3.4.1 | additional information | PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview | Saccharomyces cerevisiae | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | More | PDI domain structure, overview | Chlamydomonas reinhardtii |
| 5.3.4.1 | More | PDI domain structure, overview | Escherichia coli |
| 5.3.4.1 | More | PDI domain structure, overview | Arabidopsis thaliana |
| 5.3.4.1 | More | PDI domain structure, overview | Homo sapiens |
| 5.3.4.1 | More | PDI domain structure, overview | Saccharomyces cerevisiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | Dsb | - |
Escherichia coli |
| 5.3.4.1 | ERp28 | - |
Homo sapiens |
| 5.3.4.1 | ERp57 | - |
Homo sapiens |
| 5.3.4.1 | ERp72 | - |
Homo sapiens |
| 5.3.4.1 | More | the enzyme belongs to the Dsb family | Escherichia coli |
| 5.3.4.1 | PDI | - |
Chlamydomonas reinhardtii |
| 5.3.4.1 | PDI | - |
Escherichia coli |
| 5.3.4.1 | PDI | - |
Arabidopsis thaliana |
| 5.3.4.1 | PDI | - |
Homo sapiens |
| 5.3.4.1 | PDI | - |
Saccharomyces cerevisiae |
| 5.3.4.1 | PDIp | - |
Homo sapiens |
| 5.3.4.1 | protein disulfide isomerase | - |
Chlamydomonas reinhardtii |
| 5.3.4.1 | protein disulfide isomerase | - |
Escherichia coli |
| 5.3.4.1 | protein disulfide isomerase | - |
Arabidopsis thaliana |
| 5.3.4.1 | protein disulfide isomerase | - |
Homo sapiens |
| 5.3.4.1 | protein disulfide isomerase | - |
Saccharomyces cerevisiae |
| 5.3.4.1 | RB60 | - |
Chlamydomonas reinhardtii |
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Release 2023.1 (January 2023)
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