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Rational Engineering of Enzyme Allosteric Regulation through Sequence Evolution Analysis

Figure 4

Mutations in each allosteric site of E. coli FBPase.

(A) Residues in the allosteric regulator AMP binding site. Four residues T23, K104, Y105, and R132 have hydrogen bonds and/or polar contacts, represented by yellow dotted lines, with AMP. The mutated positions are shown in blue and cyan. In particular, less conserved residues are shown in blue. (B) Comparison of inhibition constants of wild-type and mutant FBPase by the allosteric inhibitor, AMP. The statistical significance (P-value) was measured by t-test. (C) Comparison of the catalytic efficiencies of wild-type FBPase and AMP binding site mutants. (D) Residues in the allosteric regulator Glc-6-P binding site. Five residues Y203, E207, Y210, K222, and Q225 have hydrogen bonds and/or polar contacts, represented by yellow dotted lines, with Glc-6-P; K218 interlocks with Y210. The mutated positions are shown in blue and cyan. In particular, less conserved residues are shown in blue. (E) Comparison of inhibition constant of wild-type and mutant FBPase by the allosteric inhibitor, Glc-6-P. (F) Comparison of catalytic efficiencies of wild-type FBPase and Glc-6-P binding site mutants.

Figure 4

doi: https://doi.org/10.1371/journal.pcbi.1002612.g004