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. 2000 Apr 4;97(8):3844–3849. doi: 10.1073/pnas.050588097

Table 2.

Thermodynamic coupling parameters for wild type and all three active site mutants of BsPFK at 25°C

Enzyme Kia, mM Kiy, mM Qay × 103 ΔGay, kcal/mol
Wild type 0.028  ± 0.002 0.040  ± 0.004 1.4  ± 0.1 3.89  ± 0.04
E161A 0.025  ± 0.002 0.106  ± 0.011 2.5  ± 0.7 3.55  ± 0.17
R162A 1.16   ± 0.06 1.01   ± 0.09 23    ± 4 2.23  ± 0.10
E161A/R162A 0.76   ± 0.06 0.166  ± 0.019 14   ± 1 2.53  ± 0.04

Parameters were determined from steady-state kinetics with MgATP = 3 mM.