Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer?

I Nikolic-Hughes, DC Rees…

Index: Nikolic-Hughes, Ivana; Rees, Douglas C.; Herschlag, Daniel Journal of the American Chemical Society, 2004 , vol. 126, # 38 p. 11814 - 11819

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Citation Number: 47

Abstract

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 ...