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. 2012 Sep 6;287(45):38110–38123. doi: 10.1074/jbc.M112.398180

TABLE 4.

Binding kinetics of RPV to WT and mutant enzymes

Values in parenthesis represent -fold change with respect to the WT enzyme.

Enzyme Kd.RPVa kon.RPVa koff.RPVa Kd.RPVb kon.RPVb koff.RPVb
nm nm1 s1 s1 nm nm1 s1 s1
WT 17.9 ± 2.1 (1) 0.07 ± 0.01 (1) 1.3 ± 0.2 (1) 13.9 ± 1.7 (1) 0.14 ± 0.03 (1) 1.9 ± 0.3 (1)
p66M184I/p51WT 21.1 ± 1.6 (1.2) 0.06 ± 0.01 (0.9) 1.3 ± 0.1 (0.9) 10.5 ± 1.1 (0.8) 0.18 ± 0.02 (1.3) 1.9 ± 0.3 (1)
p66E138K/p51E138K 31.9 ± 1.9 (1.8) 0.33 ± 0.02 (4.7) 9.0 ± 0.8 (7.2) 30.9 ± 2.3 (2.2) 0.32 ± 0.03 (2.3) 11.5 ± 1.8 (5.9)
p66E138K/M184I/p51E138K 36.8 ± 1.3 (2.1) 0.15 ± 0.02 (2.1) 5.3 ± 0.6 (4.2) 26.8 ± 1.9 (1.9) 0.28 ± 0.01 (2.0) 7.5 ± 1.1 (3.9)
p66M184I/p51E138K 28.4 ± 2.3 (1.6) 0.31 ± 0.01 (4.4) 5.3 ± 0.6 (4.2) 32.9 ± 2.6 (2.4) 0.29 ± 0.05 (2.1) 9.5 ± 1.2 (4.9)

a Values obtained by fitting data to Equations 46. Also, Kd.RPV = koff.RPV/kon.RPV.

b Values obtained by globally fitting the data using KinTek Explorer.