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Literature summary for 3.4.24.56 extracted from
- Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme (2009), FASEB J., 23, 3734-3742.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| nestin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Rattus norvegicus | |
| nestin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Xenopus laevis | |
| phosphorylated vimentin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Rattus norvegicus | |
| phosphorylated vimentin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Xenopus laevis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning from C6 glioma cells, expression of recombinant GST-tagged wild-type IDE, and of recombinant IDE mutant E111Q | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| nestin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Rattus norvegicus | |
| nestin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Xenopus laevis | |
| phosphorylated vimentin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Rattus norvegicus | |
| phosphorylated vimentin | insulin degradation activity of IDE is suppressed by about 50% by either nestin or phosphorylated vimentin, while the cleavage of bradykinin-mimetic peptide by IDE is increased 2 to 3fold | Xenopus laevis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Rattus norvegicus | 5829 | - |
| cytosol | - |
Xenopus laevis | 5829 | - |
| soluble | - |
Xenopus laevis | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 105000 | - |
x * 105000, SDS-PAGE | Xenopus laevis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| insulin + H2O | Rattus norvegicus | - |
insulin peptide fragments | - |
? |  |
| insulin + H2O | Xenopus laevis | - |
insulin peptide fragments | - |
? | |
| additional information | Xenopus laevis | IDE interacts with vimentin and nestin, vimentin binds IDE with a higher affinity than nestin in vitro. A nestin tail fragment interacts with insulin-degrading enzyme in Xenopus egg extracts, overview. The interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser55, the interaction between nestin and IDE is phosphorylation-independent. Nestin-mediated disassembly of vimentin IFs generates a structure capable of sequestering and modulating the activity of IDE, overview | ? | - |
? | |
| additional information | Rattus norvegicus | IDE interacts with vimentin and with nestin during mitosis, vimentin binds IDE with a higher affinity than nestin in vitro. The interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser55, the interaction between nestin and IDE is phosphorylation-independent. Nestin-mediated disassembly of vimentin IFs generates a structure capable of sequestering and modulating the activity of IDE, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
| Xenopus laevis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from oocytes | Xenopus laevis |
| recombinant GST-tagged wild-type and mutant IDEs | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| C6 glioma cell | glioma cells | Rattus norvegicus | - |
| oocyte | - |
Xenopus laevis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| insulin + H2O | - |
Rattus norvegicus | insulin peptide fragments | - |
? | |
| insulin + H2O | - |
Xenopus laevis | insulin peptide fragments | - |
? | |
| additional information | IDE interacts with vimentin and nestin, vimentin binds IDE with a higher affinity than nestin in vitro. A nestin tail fragment interacts with insulin-degrading enzyme in Xenopus egg extracts, overview. The interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser55, the interaction between nestin and IDE is phosphorylation-independent. Nestin-mediated disassembly of vimentin IFs generates a structure capable of sequestering and modulating the activity of IDE, overview | Xenopus laevis | ? | - |
? | |
| additional information | IDE interacts with vimentin and with nestin during mitosis, vimentin binds IDE with a higher affinity than nestin in vitro. The interaction between vimentin and IDE is enhanced by vimentin phosphorylation at Ser55, the interaction between nestin and IDE is phosphorylation-independent. Nestin-mediated disassembly of vimentin IFs generates a structure capable of sequestering and modulating the activity of IDE, overview | Rattus norvegicus | ? | - |
? | |
| peptide V + H2O | a bradykinin-mimetic fluorogenic peptide substrate V | Rattus norvegicus | ? | - |
? | |
| peptide V + H2O | a bradykinin-mimetic fluorogenic peptide substrate V | Xenopus laevis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 105000, SDS-PAGE | Xenopus laevis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| IDE | - |
Rattus norvegicus |
| IDE | - |
Xenopus laevis |
| Insulin-degrading enzyme | - |
Rattus norvegicus |
| Insulin-degrading enzyme | - |
Xenopus laevis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Rattus norvegicus |
| 37 | - |
assay at | Xenopus laevis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Rattus norvegicus |
| 7.4 | - |
assay at | Xenopus laevis |
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