Rationalizing the Influence of the Binding Affinity on the Activity of Phosphoserine Phosphatases
Yoko Chiba,
Hideshi Ooka,
Marie E. Wintzer
et al.
Abstract:The Sabatier principle states that catalytic activity can be maximized when the substrate binding affinity is neither too strong nor too weak. Recent studies have shown that the activity of several hydrolases is maximized at intermediate values of the binding affinity (Michaelis–Menten constant: Km). However, it remains unclear whether this concept of artificial catalysis is applicable to enzymes in general, especially for those which have evolved under different reaction environments. Herein, we show that the… Show more
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