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	
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	
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	
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