the results show that ( i ) changes in inhibitor residues other than the primary recognition residue ( p1 ) even sequentially far from the reactive site , may exert large effects on association equilibrium constant values provided these residues make contact with the enzyme , ( ii ) changes in residues other than p1 often exert large differential effects toward the different enzymes , i.e. , the same change can make the inhibitor stronger for one enzyme and weaker for another , ( iii ) the sign and to some extent the magnitude of the changes can be rationalized from the known structures of the inhibitor and the enzyme , ( iv ) changes in surface residues which do not contact the enzyme in complex are virtually without effect , and ( v ) glycosylated and nonglycosylated inhibitors have the same constants .
C0014442
enzyme
C0026741
enzyme