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. 2014 Mar 17;53(12):2053–2063. doi: 10.1021/bi4015049

Figure 2.

Figure 2

Pre-steady-state kinetic and Taft analysis of a series of acyl-CoAs. The dashed line indicates 1 equiv of enzyme: (A) acetoacetyl-CoA (R = Ac), (B) bromoacetyl-CoA (R = Br), (C) chloroacetyl-CoA (R = Cl), and (D) cyanoacetyl-CoA (R = CN). (E) Taft plot for the acylation step of FlK-catalyzed acyl-CoA hydrolysis. Acylation rate constants (k2) are derived from nonlinear curve fitting of pre-steady-state kinetic time courses. Values are reported as means ± the standard deviation (n = 3). The linear fit gave a ρ* value of 1.7 ± 0.2 (R2 = 0.986).