by Keshwani, M.M. et al.
Department of Chemistry, University of Miami, Coral Gables, Florida 33124, USA
Department of Chemistry, University of Miami, Coral Gables, Florida 33124, USA
Herein, we report direct binding and kinetic studies that showed PDK1 to exhibit nearly equal binding affinities and steady-state kinetic turnover numbers toward native (K(d)(S6K1) = 1.2 microm and k(cat) = 1.1 s(-1)) and the phosphomimicking T389E mutant S6K1 alpha II (K(d)(S6K1) = 1.5 microm and k(cat) = 1.2 s(-1)), although approximately 2-fold enhanced specificity was displayed for the T389E mutant (k(cat)/K(m)(S6K1) = 0.08 microm(-1) s(-1) compared with 0.04 microm(-1) s(-1)).
J. Biol. Chem. 2009; 34:22611-24
