EC Number   |
Reaction |
Reference |
|---|
   3.4.24.56 | Degradation of insulin, glucagon and other polypeptides. No action on proteins |
- |
- |
| 3.4.24.56 | Degradation of insulin, glucagon and other polypeptides. No action on proteins |
ability of substrates to properly anchor their N-terminus to the exosite of IDE and undergo a conformational switch upon binding to the catalytic chamber of IDE can also contribute to the selective degradation of structurally related growth factors. The high dipole moment of substrates complements the charge distribution of the IDE catalytic chamber for the substrate selectivity |
709536 |
| 3.4.24.56 | Degradation of insulin, glucagon and other polypeptides. No action on proteins |
Glu111 serves as a base to activate a catalytic water molecule within the active site of the enzyme, mediating peptide hydrolysis, mutation of this residue to glutamine renders IDE inactive, the catalytic water that is coordinated by a zinc ion also interacts with a glutamate residue, which serves as the general acid/base catalyst, catalytic mechanism |
683651 |
| 3.4.24.56 | Degradation of insulin, glucagon and other polypeptides. No action on proteins |
molecular basis of catalytic chamber-assisted unfolding and cleavage of human insulin by human insulin-degrading enzyme, IDE utilizes the interaction of its exosite with the N-terminus of the insulin A chain, overview. The unique size, shape, charge distribution, and exosite of the IDE catalytic chamber contribute to its high affinity for insulin |
709016 |
| 3.4.24.56 | Degradation of insulin, glucagon and other polypeptides. No action on proteins |
reaction mechanism, active-site model, detailed overview |
708871 |
