EC Number   |
Reaction |
Reference |
|---|
   3.4.11.9 | release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide |
- |
- |
| 3.4.11.9 | release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide |
acive site configuration, modeling, Asp449, Asp460, His523, Glu554, and Glu568 are in volved in metal binding in the active site, His429 and His523 are involved in shuttling protons during catalysis |
649942 |
| 3.4.11.9 | release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide |
H243 stabilizes substrate binding, H361 stabilizes substrate binding and the gem-diol catalytic intermediate. H350 forms part of a hydrophobic binding pocket that gives the enzyme its proline specificity |
667743 |
| 3.4.11.9 | release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide |
isozyme APP-2 shows a preference for Arg-Pro-Pro-, Arg-Pro-Lys-, Pro-Pro-Gly-, -Phe-Gly- in descending order |
652158 |
| 3.4.11.9 | release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide |
mechanism, cis-trans specificity |
-, 36048 |
| 3.4.11.9 | release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide |
R404 participates in proton relay and in the hydrogen bond network |
667712 |
