Literature summary for 3.4.24.56 extracted from

Li, P.; Kuo, W.L.; Yousef, M.; Rosner, M.R.; Tang, W.J.
The C-terminal domain of human insulin degrading enzyme is required for dimerization and substrate recognition (2006), Biochem. Biophys. Res. Commun., 343, 1032-1037.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
56000	-	x * 113000, native enzyme, x * 56000, isolated C-terminal domain IDE-C, 1 * 60000, isolated N-terminal domain IDE-N, SDS-PAGE	Homo sapiens
60000	-	x * 113000, native enzyme, x * 56000, isolated C-terminal domain IDE-C, 1 * 60000, isolated N-terminal domain IDE-N, SDS-PAGE	Homo sapiens
113000	-	x * 113000, native enzyme, x * 56000, isolated C-terminal domain IDE-C, 1 * 60000, isolated N-terminal domain IDE-N, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Subunits

Subunits	Comment	Organism
?	x * 113000, native enzyme, x * 56000, isolated C-terminal domain IDE-C, 1 * 60000, isolated N-terminal domain IDE-N, SDS-PAGE	Homo sapiens
More	enzyme may be subdivided into roughly equal sized domains IDE-C and IDE-N by limited proteolysis. Separation and analysis of domains show that IDE-N is a monomer and IDE-C serves to oligomerize IDE-N. IDE-C alone does not have catalytic activity, IDE-N alone has 2% of wild-type activity. By complexing IDE-C with IDE-N, activity can be restored to 30% of wild-type	Homo sapiens

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Release 2023.1 (January 2023)