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Quantum chemical calculations were performed with the goal of achieving a better understanding of theinfluence of Arg166 on the catalytic activity of alkaline phosphatases. The present results indicate that theactive site Arg166 residue contributes to catalysis by orienting the phosphate monoester substrate in afavorable position for the rate-limiting nucleophilic attack. The stabilizing hydrogen bond interactions of theguanidinium group with two nonbridging oxygens of the phosphate decrease the barrier for the phosphoryltransfer process by attainment of a tighter and preorganized transition state.