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Literature summary for 5.3.4.1 extracted from
- Solution structure of the bb domains of human protein disulfide isomerase (2009), FEBS J., 276, 1440-1449.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of GST-tagged bb' fragment, residues P135-S357, and of b' fragment, residues L236-S357, in Escherichia coli strain Bl21(DE3) | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | loss of the two cysteines in the C-terminal a' domain increases the Km for substarte RNase A, and loss of an additional cysteine in the a domain resulted in an even further increase of the Km | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition of PDI oxido-reductase activity with di(o-aminobenzyl)-labeled oxidized glutathione by DELTA-somatostatin | Homo sapiens | |
| Somatostatin | - |
Homo sapiens |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.007 | - |
RNAse A | wild-type PDI | Homo sapiens | |
| 0.036 | - |
RNAse A | mutant PDI without Cys in domain a' | Homo sapiens | |
| 0.05 | - |
RNAse A | mutant PDI without two Cys in domains a' and a | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | PDI catalyzes disulfide bond formation in the endoplasmic reticulum | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P07237 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GST-tagged bb' fragment and b' fragment from Escherichia coli strain Bl21(DE3) by glutathione affinity chromatography and gel filtration | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| bronchial epithelial cell | - |
Homo sapiens | - |
| lung | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | PDI catalyzes disulfide bond formation in the endoplasmic reticulum | Homo sapiens | ? | - |
? | |
| RNase A | PDI catalyzes the refolding of denatured bovine RNase A. The protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, overview | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, and interaction analysis of b and b' domains of PDI, the b' domain tends to form dimers, while the b domain moderates the tendency of the b' domain to dimerize and significantly slows interconversion, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDI | - |
Homo sapiens |
| protein disulfide isomerase | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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