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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.
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BMC Microbiology

ISSN: 1471-2180

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