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Literature summary for 5.3.4.1 extracted from
- Protein disulfide isomerase (2004), Biochim. Biophys. Acta, 1699, 35-44.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | PDI1 gene expression is stress-induced by over 2.5fold in response to e.g. reducing agents such as DTT, or to thiol-specific oxidizing agents such as diamide, other PDI gene homologues are also stress-induced | Saccharomyces cerevisiae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | PDI can rescue a PDI-deficient mutant strain as well as mutants deficient in PDI homologues Eug1p, Mpd1p, Mpd2p, and Eps1p | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | lumen, high concentration in the ER | Homo sapiens | 5783 | - |
| endoplasmic reticulum | lumen, high concentration in the ER | Rattus norvegicus | 5783 | - |
| endoplasmic reticulum | lumen, high concentration in the ER | Saccharomyces cerevisiae | 5783 | - |
| endoplasmic reticulum | lumen, high concentration in the ER | Bos taurus | 5783 | - |
| periplasm | - |
Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions | ? | - |
? |  |
| additional information | Bos taurus | modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition | ? | - |
? | |
| additional information | Homo sapiens | modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens | ? | - |
? | |
| additional information | Saccharomyces cerevisiae | regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions | ? | - |
? | |
| additional information | Escherichia coli | the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | PDI is N-glycosylated | Saccharomyces cerevisiae |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| catalyses the rearrangement of -S-S- bonds in proteins | disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states | Escherichia coli | |
| catalyses the rearrangement of -S-S- bonds in proteins | disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states | Homo sapiens | |
| catalyses the rearrangement of -S-S- bonds in proteins | disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states | Rattus norvegicus | |
| catalyses the rearrangement of -S-S- bonds in proteins | disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| B-lymphocyte | cell surface | Homo sapiens | - |
| liver | - |
Rattus norvegicus | - |
| pancreas | tissue-specific expression of PDI | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions | Rattus norvegicus | ? | - |
? | |
| additional information | modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition | Bos taurus | ? | - |
? | |
| additional information | modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens | Homo sapiens | ? | - |
? | |
| additional information | regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions | Escherichia coli | ? | - |
? | |
| additional information | DsbC and DbsG also possess thioredoxin-like domains, substrate specificity of PDI | Escherichia coli | ? | - |
? | |
| additional information | Eug1p, Mpd1p, Mpd2p, and Eps1p partially compensate for PDI, substrate specificity of PDI | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | substrate specificity of PDI | Homo sapiens | ? | - |
? | |
| additional information | substrate specificity of PDI | Rattus norvegicus | ? | - |
? | |
| additional information | substrate specificity of PDI | Bos taurus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | DsbC dimerizes to form a protein binding site flanked by two catalytic thioredoxin domains | Escherichia coli |
| More | PDI domain organization, 5 domains a, b, b', a', and c, domains a and a' are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, domain structure and electrostatic surface, overview | Rattus norvegicus |
| More | PDI domain organization, domains a, b, b', a', PDI and P5 contain both two thioredoxin-like domains, domains a and a', at the N-terminus and the C-terminus, respectively, are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, overview | Homo sapiens |
| More | PDI domain organization, Eug1p, Mpd1p, Mpd2p, and Eps1p have only one catalytic domain with 2 cysteines, overview | Saccharomyces cerevisiae |
| More | PDI domain organization, overview | Escherichia coli |
| More | PDI domain organization, overview | Bos taurus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DbsG | - |
Escherichia coli |
| DsbC | - |
Escherichia coli |
| Eps1p | - |
Saccharomyces cerevisiae |
| Eug1p | - |
Saccharomyces cerevisiae |
| More | PDI belongs to the thioredoxin superfamily | Homo sapiens |
| More | PDI belongs to the thioredoxin superfamily | Rattus norvegicus |
| More | PDI belongs to the thioredoxin superfamily | Bos taurus |
| More | PDI, DsbC, and DbsG belong to the thioredoxin superfamily | Escherichia coli |
| More | PDI, Eug1p, Mpd1p, Mpd2p, and Eps1p belong to the thioredoxin superfamily | Saccharomyces cerevisiae |
| Mpd1p | - |
Saccharomyces cerevisiae |
| Mpd2p | - |
Saccharomyces cerevisiae |
| P5 | PDI homologue | Homo sapiens |
| PDI | - |
Escherichia coli |
| PDI | - |
Homo sapiens |
| PDI | - |
Rattus norvegicus |
| PDI | - |
Saccharomyces cerevisiae |
| PDI | - |
Bos taurus |
| PDI1 | - |
Saccharomyces cerevisiae |
| protein disulfide isomerase | - |
Escherichia coli |
| protein disulfide isomerase | - |
Homo sapiens |
| protein disulfide isomerase | - |
Rattus norvegicus |
| protein disulfide isomerase | - |
Saccharomyces cerevisiae |
| protein disulfide isomerase | - |
Bos taurus |
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Release 2023.1 (January 2023)
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