Effect of Pressure on Catalytic Properties of Glutamate Racemase from Aquifex pyrophilus, an Extremophilic Bacteria

  • Lee, Ki-Seog (Division of Biotechnology and Genetic Engineering, Korea University) ;
  • Chi, Young-Min (Division of Biotechnology and Genetic Engineering, Korea University) ;
  • Yu, Yeon-Gyu (Structural Biology Center, Korea Institute of Science and Technology)
  • Published : 2002.02.01

Abstract

The effect of pressure on the catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacterium, was investigated. The activation volume for the overall reaction $({\Delta}V^{\neq})$ and catalysis $({{Delta}V_{cat}}^{\neq})$ was -96.97 ml/mol and 4.97 ml/mol, respectively, while the reaction volume for the substrate binding (${\Delta}V_{K_m^-1}$) was -101.94 ml/mol. The large negative ${\Delta}V^{\neq}$ for the overall reaction indicated that the pressurization of glutamate racemase resulted in enhanced catalytic efficiencies. In addition, this value was also due to the large negative ${Delta}V_{K_m^-1}$ for the substrate binding. The negative value of ${Delta}V_{K_m^-1}$ implied that the conformational changes in the enzyme molecule occurred during the substrate binding process, thereby increasing the degree of hydration. The small value of ${{Delta}V_{cat}}^{\neq}$suggested that the pressure did not affect the glutamate racemase catalysis after the substrate binding.

Keywords

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