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Literature summary extracted from

  • Perlman, R.K.; Gehm, B.D.; Kuo, W.L.; Rosner, M.R.
    Functional analysis of conserved residues in the active site of insulin-degrading enzyme (1993), J. Biol. Chem., 268, 21538-21544.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.56 additional information not: the enzyme is inhibited by cysteine protease inhibitors as well as metalloprotease inhibitors Drosophila melanogaster
3.4.24.56 additional information not: the enzyme is inhibited by cysteine protease inhibitors as well as metalloprotease inhibitors Homo sapiens
3.4.24.56 additional information not: the enzyme is inhibited by cysteine protease inhibitors as well as metalloprotease inhibitors Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.56 Drosophila melanogaster
-
-
-
3.4.24.56 Homo sapiens
-
-
-
3.4.24.56 Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.56 Insulin + H2O
-
 Drosophila melanogaster Hydrolyzed insulin
-
 ?
3.4.24.56 Insulin + H2O
-
 Homo sapiens Hydrolyzed insulin
-
 ?
3.4.24.56 Insulin + H2O
-
 Rattus norvegicus Hydrolyzed insulin
-
 ?
3.4.24.56 additional information
-
 Rattus norvegicus ?
-
 ?
3.4.24.56 additional information the conserved glutamate in the zinc-binding site of human enzyme is a major catalytic residue, while a conserved cysteine in this region is not essential for catalysis Homo sapiens ?
-
 ?