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Rational Engineering of Enzyme Allosteric Regulation through Sequence Evolution Analysis

Figure 5

Combinatorial mutations of allosteric sites of E. coli FBPase.

(A) Comparison of inhibition constants of wild-type and mutant FBPase by AMP and Glc-6-P. The statistical significance (P-value) was measured by t-test. (B) Comparison of catalytic efficiencies of wild-type and mutant FBPase. (C) The profile of catalytic activities of wild-type and mutant FBPase in the presence of various concentrations of AMP and Glc-6-P. The range of AMP concentrations was 0–500 µM and that of Glc-6-P was 0–5000 µM.

Figure 5