Literature summary for 3.4.24.56 extracted from

Llovera, R.E.; de Tullio, M.; Alonso, L.G.; Leissring, M.A.; Kaufman, S.B.; Roher, A.E.; de Prat Gay, G.; Morelli, L.; Castano, E.M.
The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: implications for Alzheimer disease pathogenesis (2008), J. Biol. Chem., 283, 17039-17048.

Search for more literature for 3.4.24.56

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	native enzyme, insulysin is able to form a stable complex with amyloid beta	Rattus norvegicus	-

Subunits

Subunits	Comment	Organism
More	both recombinant and brain enzyme are able to form a stable complex with amyloid beta that resists dissociation after treatment with strong denaturants. Amyloid beta sequence 17-27 is sufficient to form a stable complex with IDE. Monomeric as opposed to aggregated amyloid beta is competent to associate irreversibly with IDE following a very slow kinetics. Partial denaturation of IDE as well as preincubation with a 10fold molar excess of insulin prevent complex formation. Amyloid beta remains bound to a 25 kDa N-terminal fragment of IDE in an SDS-resistant manner	Rattus norvegicus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)