Functional properties and hydrodynamic diameter of AGT variants.

aEnzyme kinetic parameters were obtained from global fittings of 2–4 independent experimental series using a double-displacement mechanism;bKd values were estimated from single titrations except for AGT WT protein where Kd value is the mean±s.d. from three independent titrations. Data in parenthesis are Kd estimates obtained from the kinetic binding experiments (Kd = koff/kon).cHydrodynamic diameter of holo-AGT variants determined by dynamic light scattering (DLS). Data are mean±s.d. of 3–9 independent measurements.