Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP hydrolysis is a mechanism for reversion of this inhibition, however, insulin does not modify the ATPase activity of IDE | Rattus norvegicus | |
EDTA | - |
Rattus norvegicus | |
Li+ | inhibits at 1 mM | Rattus norvegicus | |
Mg2+ | activates, less active than Mn2+, inhibitory at above 0.05 mM | Rattus norvegicus | |
orthovanadate | inhibits ATP hydrolysis and insulin degradation | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.063 | - |
ATP | pH 7.4, 37°C | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates at concentration up to 0.05 mM, less active than Mn2+, inhibitory at above 0.05 mM | Rattus norvegicus | |
Mn2+ | activates, best at 1 mM, preferred divalent cation for both insulin degradation and ATP hydrolysis | Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
110000 | - |
gel filtration | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Rattus norvegicus | insulin-binding and degradation are dependent on ATP concentration, however, insulin does not modify the ATPase activity of IDE | ADP + phosphate | - |
? | |
insulin + H2O | Rattus norvegicus | degradation, insulin-binding and degradation are dependent on ATP concentration, however, insulin does not modify the ATPase activity of IDE | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
male Wistar rats | - |
Purification (Comment) | Organism |
---|---|
native enzyme from skeletal muscle by anion exchange chromatography and chromatofocusing to homogeneity | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | recombinant enzyme | Rattus norvegicus | - |
skeletal muscle | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | insulin-binding and degradation are dependent on ATP concentration, however, insulin does not modify the ATPase activity of IDE | Rattus norvegicus | ADP + phosphate | - |
? | |
ATP + H2O | the enzyme contains one ATP binding site per enzyme molecule | Rattus norvegicus | ADP + phosphate | - |
? | |
insulin + H2O | degradation, insulin-binding and degradation are dependent on ATP concentration, however, insulin does not modify the ATPase activity of IDE | Rattus norvegicus | ? | - |
? | |
insulin + H2O | porcine substrate, degradation | Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 110000, SDS-PAGE | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
IDE | - |
Rattus norvegicus |
Insulin-degrading enzyme | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Rattus norvegicus |