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Literature summary for 3.4.24.56 extracted from

  • Camberos, M.d.; Cresto, J.C.
    Insulin-degrading enzyme hydrolyzes ATP (2007), Exp. Biol. Med., 232, 281-292.
    View publication on PubMed

Inhibitors

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.063
-
ATP pH 7.4, 37°C Rattus norvegicus

Metals/Ions

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 [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Rattus norvegicus
-
male Wistar rats
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from skeletal muscle by anion exchange chromatography and chromatofocusing to homogeneity Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation recombinant enzyme Rattus norvegicus
-
skeletal muscle
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
monomer 1 * 110000, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
IDE
-
Rattus norvegicus
Insulin-degrading enzyme
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Rattus norvegicus