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. 2006 Feb;188(3):1143–1154. doi: 10.1128/JB.188.3.1143-1154.2006

TABLE 6.

Thermodynamic parameters of acetyl phosphate binding to wild-type and variant phosphotransacetylases

Enzyme na KD (μM) ΔH (kcal mol−1) ΔG (kcal mol−1)
Wild type 1 180 ± 10 −8.1 ± 0.2 −5.1
Arg310Gln 1 670 ± 20 −12.0 ± 3 −4.3
Arg310Lys 1 1,010 ± 20 −10.0 ± 0.1 −4.1
a

The values extracted from the data sets for “n” ranged from 0.8 to 1.3 and were fixed at 1 for consistent curve fitting.