159700-65-9Relevant academic research and scientific papers
A thermodynamic study of the conversion of chorismate to isochorismate
Tewari, Yadu B.,Davis, Andrew M.,Reddy, Prasad,Goldberg, Robert N.
, p. 1057 - 1070 (2000)
Microcalorimetry and high performance liquid chromatography were used to conduct a thermodynamic investigation of the biochemical reaction chorismate(aq) = isochorismate(aq). This reaction occurs at the branch point of the chorismate metabolic pathway that leads to the synthesis of enterobactin. Isochorismate synthase, the enzyme that catalyzesthis reaction, was prepared for this study by using molecular biology techniques. The equilibrium and calorimetric measurements were performed at T = 298.15 K and at the respective pHs 7.34 and 6.93. For the chemical reference reaction chorismate2-(aq) = isochorismate2-(aq), the equilibrium constant K = (0.84 ± 0.04) and the standard molar enthalpy of reaction ΔrHmo = -(0.81 ± 0.27) kJ · mol-1 at T = 298.15 K and ionic strength lm = 0. Under approximately physiological conditions, the apparent equilibrium constant K′ = 0.83 and the standard transformed Gibbs energy change ΔrG′mo = 0.48 kJ · mol-1 for the overall biochemical reaction.
Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase
Jiang, Ming,Guo, Zhihong
, p. 730 - 731 (2007/10/03)
Macromolecular crowding was found to significantly enhance the intrinsic catalytic efficiency of the enterobactin-specific isochorismate synthase by inducing structural change in the enzyme. This finding provides the first experimental evidence that macro
