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Literature summary extracted from
- Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin (2002), J. Biol. Chem., 277, 310-317.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.3.4.1 | expression in Escherichia coli | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.4.1 | genistein | suppresses binding of proinsulin to PDI, inhibits 66% of PDIs chaperone activity | Homo sapiens |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.4.1 | Homo sapiens | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.3.4.1 | recombinant PDI | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.4.1 | unfolded proinsulin | PDI acts both as a chaperone and as an isomerase during folding and disulfid bond formation of proinsulin, chaperone and isomerization activity is required at the beginning of proinsulin folding, the late refolding process only depends on the isomerase activity | Homo sapiens | refolded proinsulin | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.4.1 | PDI | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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