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Table 2 Kinetic and thermodynamic data of Emodin binding to HpFabZ

From: Emodin targets the β-hydroxyacyl-acyl carrier protein dehydratase from Helicobacter pylori: enzymatic inhibition assay with crystal structural and thermodynamic characterization

Kinetic Data*  
R max (RU) 42.3 ± 1.51
k a (per M per s) 4.21 × 104 ± 0.273
k d (per s) 0.193 ± 0.0061
K D (μM) 4.59
Chi2 1.64
Thermodynamic Data**  
N 1.07 ± 0.035
K D ' (μM) 0.45
ΔH (kcal/mol) -17.77 ± 1.11
TΔS (kcal/mol) -9.12
  1. * R max , maximum analyte binding capacity; K a , association rate constant; K d , dissociation rate constant; K D , equilibrium dissociation constant determined by SPR; Chi2, statistical value in BIAevaluation; ** N, stoichiometry of Emodin-HpFabZ complex; K D ', equilibrium dissociation constant determined by ITC.