EC Number   |
Reaction |
Reference |
|---|
   3.4.23.16 | specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro |
flap closing and conformational change mechanism induced by substrate binding in HIV-1 aspartic protease, flap conformations in the active site during the catalytic cycle, molecular dynamic simulations, overview |
664137 |
| 3.4.23.16 | specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro |
proteolysis mechanism whereby only one active site Asp is initially protonated. The steps of this mechanism are: asymmetric binding of the substrate, hydration of the peptidic carbonyl by an active site water, proton translocation between the active site Asp residue simultaneously with carbonyl hydration |
648146 |
| 3.4.23.16 | specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro |
the active site structure and conformational flexibility |
666873 |
| 3.4.23.16 | specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro |
the kinetic mechanism of HIV-1 protease is random, in which products bind to form both binary and ternary enzyme-product complexes, depending on the substrate used |
648124 |
