Kinetic parameters for pol λ-tdt inhibition by the three DKHA derivatives Different enzyme-substrate complexes were tested as outlined in Fig. 2 and under Materials and Methods, and equilibrium dissociation constants for inhibitor binding to the different enzymatic forms are as described there. k2 indicates apparent affinity of the enzyme for the nucleotide substrate in the presence of the inhibitor, k-2 indicates association and dissociation rates for the nucleotide substrate in the absence of the inhibitor, and indicates dissociation rate for the nucleotide substrate in the presence of the inhibitor. For details see text. Values are the means of three independent experiments ± S.D.