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Literature summary extracted from
- Biological functions of protein disulfide isomerase as a target of phenolic endocrine-disrupting chemicals (2010), J. Health Sci., 56, 1-13.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.4.1 | overexpression of PDI in GH3 cells, that release growth hormone via the T3-receptor, leads to reduced T3-induced GH release in the cells, mechanism, overview | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | 3,3',5-triiodo-L-thyronine | inhibits PDI isomerase activity | Homo sapiens |  |
| 5.3.4.1 | 3,3',5-triiodo-L-thyronine | inhibits PDI isomerase activity | Mus musculus | |
| 5.3.4.1 | 3,3',5-triiodo-L-thyronine | inhibits PDI isomerase activity | Rattus norvegicus | |
| 5.3.4.1 | 3,4-dichlorophenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Homo sapiens | |
| 5.3.4.1 | 3,4-dichlorophenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Mus musculus | |
| 5.3.4.1 | 3,4-dichlorophenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Rattus norvegicus | |
| 5.3.4.1 | 4-nonylphenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Homo sapiens | |
| 5.3.4.1 | 4-nonylphenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Mus musculus | |
| 5.3.4.1 | 4-nonylphenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Rattus norvegicus | |
| 5.3.4.1 | 4-octylphenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Homo sapiens | |
| 5.3.4.1 | 4-octylphenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Mus musculus | |
| 5.3.4.1 | 4-octylphenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Rattus norvegicus | |
| 5.3.4.1 | bisphenol A | i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview. Inhibits also PDI family members ERp57 and ERp72 | Homo sapiens | |
| 5.3.4.1 | bisphenol A | i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview | Mus musculus | |
| 5.3.4.1 | bisphenol A | i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview | Rattus norvegicus | |
| 5.3.4.1 | Pentachlorophenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Homo sapiens | |
| 5.3.4.1 | Pentachlorophenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Mus musculus | |
| 5.3.4.1 | Pentachlorophenol | inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Rattus norvegicus | |
| 5.3.4.1 | tetrabromobisphenyl A | TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Homo sapiens | |
| 5.3.4.1 | tetrabromobisphenyl A | TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Mus musculus | |
| 5.3.4.1 | tetrabromobisphenyl A | TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Rattus norvegicus | |
| 5.3.4.1 | tetrachlorobisphenyl A | TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Homo sapiens | |
| 5.3.4.1 | tetrachlorobisphenyl A | TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Mus musculus | |
| 5.3.4.1 | tetrachlorobisphenyl A | TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity | Rattus norvegicus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 5.3.4.1 | endoplasmic reticulum | - |
Mus musculus | 5783 | - |
| 5.3.4.1 | endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
| 5.3.4.1 | endoplasmic reticulum | - |
Rattus norvegicus | 5783 | - |
| 5.3.4.1 | membrane | associated | Mus musculus | 16020 | - |
| 5.3.4.1 | membrane | associated | Homo sapiens | 16020 | - |
| 5.3.4.1 | membrane | associated | Rattus norvegicus | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | Ca2+ | possibly bound at the C-terminal extension | Mus musculus | |
| 5.3.4.1 | Ca2+ | possibly bound at the C-terminal extension | Homo sapiens | |
| 5.3.4.1 | Ca2+ | possibly bound at the C-terminal extension | Rattus norvegicus | |
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 | Mus musculus | PDI specifically binds 3,3',5-triiodo-L-thyronine | ? | - |
? | |
| 5.3.4.1 | additional information | Homo sapiens | PDI specifically binds 3,3',5-triiodo-L-thyronine | ? | - |
? | |
| 5.3.4.1 | additional information | Rattus norvegicus | PDI specifically binds 3,3',5-triiodo-L-thyronine | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | Homo sapiens | - |
- |
- |
| 5.3.4.1 | Mus musculus | - |
- |
- |
| 5.3.4.1 | Rattus norvegicus | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | brain | - |
Rattus norvegicus | - |
| 5.3.4.1 | GH3 cell | a pituitary carcinoma celll line | Rattus norvegicus | - |
| 5.3.4.1 | pituitary gland | - |
Mus musculus | - |
| 5.3.4.1 | pituitary gland | - |
Homo sapiens | - |
| 5.3.4.1 | pituitary gland | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.4.1 | additional information | PDI specifically binds 3,3',5-triiodo-L-thyronine | Mus musculus | ? | - |
? | |
| 5.3.4.1 | additional information | PDI specifically binds 3,3',5-triiodo-L-thyronine | Homo sapiens | ? | - |
? | |
| 5.3.4.1 | additional information | PDI specifically binds 3,3',5-triiodo-L-thyronine | Rattus norvegicus | ? | - |
? | |
| 5.3.4.1 | additional information | the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension | Mus musculus | ? | - |
? | |
| 5.3.4.1 | additional information | the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension | Homo sapiens | ? | - |
? | |
| 5.3.4.1 | additional information | the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension | Rattus norvegicus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | More | the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview | Mus musculus |
| 5.3.4.1 | More | the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview | Homo sapiens |
| 5.3.4.1 | More | the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview | Rattus norvegicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | ERp28 | - |
Homo sapiens |
| 5.3.4.1 | ERp44 | - |
Homo sapiens |
| 5.3.4.1 | ERp57 | - |
Homo sapiens |
| 5.3.4.1 | ERp72 | - |
Homo sapiens |
| 5.3.4.1 | P5 | - |
Homo sapiens |
| 5.3.4.1 | PDI | - |
Homo sapiens |
| 5.3.4.1 | PDI | - |
Rattus norvegicus |
| 5.3.4.1 | PDIp | - |
Homo sapiens |
| 5.3.4.1 | PDIr | - |
Homo sapiens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | physiological function | PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview | Mus musculus |
| 5.3.4.1 | physiological function | PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview | Homo sapiens |
| 5.3.4.1 | physiological function | PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview | Rattus norvegicus |
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