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Literature summary extracted from
- Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme (2009), FASEB J., 23, 3734-3742.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.56 | 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 | |
| 3.4.24.56 | 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 | |
| 3.4.24.56 | 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 | |
| 3.4.24.56 | 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.24.56 | cloning from C6 glioma cells, expression of recombinant GST-tagged wild-type IDE, and of recombinant IDE mutant E111Q | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.56 | 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 | |
| 3.4.24.56 | 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 | |
| 3.4.24.56 | 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 | |
| 3.4.24.56 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.56 | cytosol | - |
Rattus norvegicus | 5829 | - |
| 3.4.24.56 | cytosol | - |
Xenopus laevis | 5829 | - |
| 3.4.24.56 | soluble | - |
Xenopus laevis | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.56 | 105000 | - |
x * 105000, SDS-PAGE | Xenopus laevis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.56 | insulin + H2O | Rattus norvegicus | - |
insulin peptide fragments | - |
? |  |
| 3.4.24.56 | insulin + H2O | Xenopus laevis | - |
insulin peptide fragments | - |
? | |
| 3.4.24.56 | 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 | ? | - |
? | |
| 3.4.24.56 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.56 | Rattus norvegicus | - |
- |
- |
| 3.4.24.56 | Xenopus laevis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.24.56 | native enzyme from oocytes | Xenopus laevis |
| 3.4.24.56 | recombinant GST-tagged wild-type and mutant IDEs | Rattus norvegicus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.24.56 | C6 glioma cell | glioma cells | Rattus norvegicus | - |
| 3.4.24.56 | oocyte | - |
Xenopus laevis | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.56 | insulin + H2O | - |
Rattus norvegicus | insulin peptide fragments | - |
? | |
| 3.4.24.56 | insulin + H2O | - |
Xenopus laevis | insulin peptide fragments | - |
? | |
| 3.4.24.56 | 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 | ? | - |
? | |
| 3.4.24.56 | 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 | ? | - |
? | |
| 3.4.24.56 | peptide V + H2O | a bradykinin-mimetic fluorogenic peptide substrate V | Rattus norvegicus | ? | - |
? | |
| 3.4.24.56 | peptide V + H2O | a bradykinin-mimetic fluorogenic peptide substrate V | Xenopus laevis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.24.56 | ? | x * 105000, SDS-PAGE | Xenopus laevis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.56 | IDE | - |
Rattus norvegicus |
| 3.4.24.56 | IDE | - |
Xenopus laevis |
| 3.4.24.56 | Insulin-degrading enzyme | - |
Rattus norvegicus |
| 3.4.24.56 | Insulin-degrading enzyme | - |
Xenopus laevis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.56 | 37 | - |
assay at | Rattus norvegicus |
| 3.4.24.56 | 37 | - |
assay at | Xenopus laevis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.56 | 7.4 | - |
assay at | Rattus norvegicus |
| 3.4.24.56 | 7.4 | - |
assay at | Xenopus laevis |
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