Activating Compound | Comment | Organism | Structure |
---|---|---|---|
2'-O-(2,4,6-trinitrophenyl) adenosine triphosphate | ATP-derivative TNP-ATP | Rattus norvegicus | |
3'-O-(2,4,6-trinitrophenyl) adenosine triphosphate | ATP-derivative TNP-ATP | Rattus norvegicus | |
ATP | regulatory cationic binding site, 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, retain the ability to bind ATP, 4fold activation at 4 mM of 56 kDa fragment, poor activation of the 76 kDa enzyme fragment, overview | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
expression of the N-terminally His6-tagged enzyme in Spodopterafrugiperda Sf9 cells using the baculovirus transfection system | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0059 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, 56 kDa detagged fragment of recombinant His6-tagged enzyme | Rattus norvegicus | |
0.0075 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, 76 kDa detagged fragment of recombinant His6-tagged enzyme | Rattus norvegicus | |
0.0254 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, recombinant His6-tagged full-length enzyme | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
amyloid beta-peptide 1-40 + H2O | Rattus norvegicus | - |
? | - |
? | |
beta-endorphin + H2O | Rattus norvegicus | - |
? | - |
? | |
insulin + H2O | Rattus norvegicus | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | treatment of the recombinant N-terminally His6-tagged IDE with proteinase K leads to the initial cleavage of the His tag and linker region, followed by C-terminal cleavages resulting in intermediate fragments of 95 and 76 kDa and finally a relatively stable 56 kDa fragment, overview | Rattus norvegicus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activities of recombinant His-tagged full-length enzyme and detagged recombinant enzyme fragments with different substrates, overview | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Abz-GGFLRKHGQ-EDDnp + H2O | synthetic fluorogenic substrate | Rattus norvegicus | Abz-GGFLR + KHGQ-EDDnp | - |
? | |
amyloid beta-peptide 1-40 + H2O | - |
Rattus norvegicus | ? | - |
? | |
amyloid beta-peptide 1-40 + H2O | 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, exhibit a low level of catalytic activity but retain the ability to bind the substrate with a similar affinity as the full-length enzyme, and they retain the regulatory cationic binding site that binds ATP | Rattus norvegicus | ? | - |
? | |
beta-endorphin + H2O | - |
Rattus norvegicus | ? | - |
? | |
beta-endorphin + H2O | 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, exhibit a low level of catalytic activity but retain the ability to bind the substrate with a similar affinity as the full-length enzyme, and they retain the regulatory cationic binding site that binds ATP | Rattus norvegicus | ? | - |
? | |
insulin + H2O | - |
Rattus norvegicus | ? | - |
? | |
insulin + H2O | 76 kDa and 56 kDa fragments of IDE, derived from cleavage with proteinase K, exhibit a low level of catalytic activity but retain the ability to bind the substrate with a similar affinity as the full-length enzyme, and they retain the regulatory cationic binding site that binds ATP | Rattus norvegicus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IDE | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assya at | Rattus norvegicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.72 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, 56 kDa detagged fragment of recombinant His6-tagged enzyme | Rattus norvegicus | |
0.77 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, 76 kDa detagged fragment of recombinant His6-tagged enzyme | Rattus norvegicus | |
93.17 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, recombinant His6-tagged full-length enzyme | Rattus norvegicus | |
104 | - |
Abz-GGFLRKHGQEDDnp | pH 7.4, 37°C, recombinant His6-tagged full-length enzyme | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Rattus norvegicus |