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. 2013 Jul 24;6:105. doi: 10.1186/1754-6834-6-105

Table 3.

Activation energies and binding enthalpies for the kinetic parameters of β-glucosidases

 
 Activation energy, Ea (kJ mol-1)a
 Binding enthalpy, ΔH0 (kJ mol-1)a
  kcat(h) kcat(h)/KM(h) KM(h) Ki(Glc)
N188BG
 47.6 ± 1.3
 29.5 ± 1.7
 18.1 ± 1.0
 19.6
TaBG3
 39.8 ± 1.9
 26.2 ± 2.3
 13.6 ± 1.2
 22.8
AtBG3 48.2 ± 2.7 20.5 ± 2.4 27.7 ± 3.3 24.6

aFor the parameter p, the activation energy (for kcat(h) and kcat(h)/KM(h)) and standard binding enthalpy (for KM(h) and Ki(Glc)) was obtained from the slope of the line in the coordinates of ln(p) versus 1/T. For the data, see Additional file 1: Figure S1.