The effect of electrostatic interactions on the transition-state character for enzymatic phosphoryl transfer has been a subject of much debate. In this work, we investigate the transition state for alkaline phosphatase (AP) using linear free-energy relationships (LFERs). We determined k cat/KM for a series of aryl sulfate ester monoanions to obtain the Brønsted coefficient, βlg, and compared the value to that obtained previously for a series of aryl ...
