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Literature summary for 5.3.4.1 extracted from
- Molecular cloning, expression and characterization of protein disulfide isomerase from Conus marmoreus (2007), FEBS J., 274, 4778-4787.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GSH | - |
Conus marmoreus |  |
| NADPH | - |
Conus marmoreus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and anaylsis, phylogenetic tree, expression in Escherichia coli as a soluble cytoplasmic protein | Conus marmoreus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | the enzyme contains an N-terminal ER retention signal sequence | Conus marmoreus | 5783 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Conus marmoreus | in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Conus marmoreus | Q1HGL1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli to homogeneity and over 95% purity | Conus marmoreus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| conotoxins sTx3.1 | disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin | Conus marmoreus | ? | - |
? | |
| conotoxins tx3a | disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin | Conus marmoreus | ? | - |
? | |
| lysozyme | PDI exhibits both chaperone and antichaperone activities when catalyzing the refolding of reduced/denatured lysozyme in HEPES buffer, effect of macromolecular crowding on the PDI-catalyzed folding, overview | Conus marmoreus | ? | - |
? | |
| additional information | in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase | Conus marmoreus | ? | - |
? | |
| additional information | the enzyme shows oxidase and isomerase activities, overview | Conus marmoreus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDI | - |
Conus marmoreus |
| protein disulfide isomerase | - |
Conus marmoreus |
| thiol-protein oxidoreductase | - |
Conus marmoreus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
isomerase activity assay at | Conus marmoreus |
| 8 | - |
refolding activity assay at | Conus marmoreus |
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