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Literature summary for 3.4.24.56 extracted from

  • Bennett, R.G.; Duckworth, W.C.; Hamel, F.G.
    Degradation of amylin by insulin-degrading enzyme (2000), J. Biol. Chem., 275, 36621-36625.
    View publication on PubMed

Application

Application Comment Organism
medicine the Alzheimer's beta-amyloid peptide is degraded by the enzyme Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Rattus norvegicus
adrenocorticotropic hormone competitive inhibition of amylin degradation Rattus norvegicus
amylin excess amylin inhibits amylin degradation, competitive inhibition Rattus norvegicus
Aprotinin 22.4% inhibition Rattus norvegicus
atrialnatriuretic peptide competitive inhibition of amylin degradation Rattus norvegicus
bacitracin
-
Rattus norvegicus
EDTA 21% inhibition; 35.7% inhibition Rattus norvegicus
glucagon competitive inhibition of amylin degradation Rattus norvegicus
Insulin inhibits amylin degradation, excess insulin inhibits insulin degradation Rattus norvegicus
additional information pepstatin-A, leupeptin, and calpains are ineffective as inhibitors, no competitive inhibition with EGF or insulin C-peptide Rattus norvegicus
N-ethylmaleimide
-
Rattus norvegicus
PMSF 14.4% inhibition Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
SDS-PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
rat, Sprague-Dawley
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylin + H2O
-
Rattus norvegicus ?
-
?
beta-amyloid peptide + H2O
-
Rattus norvegicus ?
-
?
insulin + H2O
-
Rattus norvegicus ?
-
?
additional information EGF and insulin C-peptide are no substrates Rattus norvegicus ?
-
?

Synonyms

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