Effect of Pressure and Solvent Dielectric Constant on the Kinetic Constants of Trypsin-Catalyzed Reaction.

Trypsin 반응에 대한 용매의 유전상수 및 압력의 영향

  • Park, Hyun (Department of Agricultural Chemistry, College of Natural Resources, Korea University) ;
  • Chi, Young-Min (Department of Agricultural Chemistry, College of Natural Resources, Korea University)
  • 박현 (고려대학교 응용생명환경화학과) ;
  • 지영민 (고려대학교 응용생명환경화학과)
  • Published : 2000.02.01


Electrostatic forces contribute to the high degree of enzyme transition state complementarity in enzyme catalyzed reaction and such forces are modified by the solvent through its dielectric constant and polar properties. The contributions of electrostatic interaction to the formation of ES complex and the stabilization of transition state of the trypsin catalyzed reaction were probed by kinetic studied with high pressure and solvent dielectric constant. A good correlation has been observed between the increase of catalytic efficiency of trypsin and the decrease of solvent dielectric constant. Activation volume linearly decreased as the dielectric constant of solvent decreased, which means the increase in the reaction rae. Moreover, the decrease of activation volume by lowering the solvent dielectric constant implies a solvent penetration of the active with and a reduction of electrostatic energy for the formation of dipole of the active site oxyanion hole. When the 야electric constant of the solvents was lowered to 4.7 unit, the loss of activation energy and that of free energy of activation were 2.262 KJ/mol and 3.169 KJ/mol, respectively. The results of this study indicate that the high pressure kinetics combined with solvent effects can provide unique information on enzyme reaction mechanisms, and the controlling the solvent dielectric constant can stabilize the transition state of the trypsin-catalyzed reaction.



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