EC Number   |
Natural Substrates |
|---|
   3.4.24.63 | ADAM10 + H2O |
i.e. a disintegrin and metalloproteinase 10 |
| 3.4.24.63 | ADAM17 + H2O |
i.e. a disintegrin and metalloproteinase 17 |
| 3.4.24.63 | ADAM9 + H2O |
i.e. a disintegrin and metalloproteinase 9 |
| 3.4.24.63 | alpha-secretase + H2O |
meprin beta-mediated activation of the alpha-secretase |
| 3.4.24.63 | amyloid precursor protein + H2O |
- |
| 3.4.24.63 | amyloid precursor protein + H2O |
meprin beta cleaves amyloid precursor protein at the beta-secretase site, giving rise to amyloidogenic peptides |
| 3.4.24.63 | amyloid precursor protein + H2O |
APP, cleavage mechanism by meprin beta, overview |
| 3.4.24.63 | amyloid precursor protein + H2O |
APP, the precursor protein is cleaved by meprin beta in distinct ways, either at the beta-secretase site resulting in increased levels of amyloid beta (Abeta) peptides, or at the N-terminus releasing 11 kDa, and 20 kDa peptide fragments. The N-terminal 11 kDa and 20 kDa peptide fragments represent physiological cleavage products |
| 3.4.24.63 | amyloid precursor protein + H2O |
metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants |
| 3.4.24.63 | amyloid precursor protein + H2O |
meprin beta initially sheds amyloid precursor protein, releasing different amyloid beta species with several cleavage sites identical with or proximal to the known beta-secretase cleavage site |
