Alkaline Phosphatase (AP) is a ubiquitous enzyme capable of cross catalyzing the cleavage of a wide variety of phosphate and sulfate esters. In Escherichia coli AP, mutation of active site residues D153G and D330N by Le Du et. al. increased enzyme activity forty-fold yielding a prokaryotic version of the enzyme capable of attaining catalytic rates rivaling eukaryotic AP. We have found this set of mutations yield not only and increase in catalytic velocity, but also an increase in catalytic efficiency and promiscuity related to an increase in enzyme flexibility. These results are surprising given the integral role that D153 plays in stabilizing an active site triad responsible for the positioning of the phosphate functional group for cleavage.

Relaxing a catalytic triad in alkaline phosphatase

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