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Literature summary for 3.4.24.56 extracted from

  • Hubin, E.; Cioffi, F.; Rozenski, J.; van Nuland, N.A.; Broersen, K.
    Characterization of insulin-degrading enzyme-mediated cleavage of Abeta in distinct aggregation states (2016), Biochim. Biophys. Acta, 1860, 1281-1290 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
amyloid-beta + H2O Homo sapiens activity is driven by the dynamic equilibrium between Abeta monomers and higher ordered aggregates. Met35-Val36 is a cleavage site in the amyloid-beta sequence. Amyloid-beta fragments resulting from cleavage by insulin-degrading enzyme form non-toxic amorphous aggregates ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens P14735
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amyloid-beta + H2O activity is driven by the dynamic equilibrium between Abeta monomers and higher ordered aggregates. Met35-Val36 is a cleavage site in the amyloid-beta sequence. Amyloid-beta fragments resulting from cleavage by insulin-degrading enzyme form non-toxic amorphous aggregates Homo sapiens ?
-
?
amyloid-beta + H2O amyloid-beta monomers, either alone in solution or in dynamic equilibrium with higher aggregates, are cleaved at multiple sites by activity of insulin-degrading enzyme. Met35-Val36 is a cleavage site in the amyloid-beta sequence. Amyloid-beta fragments resulting from cleavage by insulin-degrading enzyme form non-toxic amorphous aggregates Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
IDE
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Homo sapiens
Insulin-degrading enzyme
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Homo sapiens