Effect of pressure and solvent dielectric constant on the kinetic constants of trypsin-catalyzed reaction

Hyun Park, Young Min Chi

Research output: Contribution to journalArticle

Abstract

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 studies 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 rate. Moreover, the decrease of activation volume by lowering the solvent dielectric constant implies a solvent penetration of the active site and a reduction of electrostatic energy for the formation of dipole of the active site oxyanion hole. When the dielectric 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.

Original languageEnglish
Pages (from-to)26-32
Number of pages7
JournalKorean Journal of Applied Microbiology and Biotechnology
Volume28
Issue number1
Publication statusPublished - 2000 Feb 1

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Trypsin
Pressure
Static Electricity
Catalytic Domain
Enzymes

Keywords

  • Dielectric constant
  • Electrostatic interaction
  • High-pressure kinetics
  • Transition state
  • Trypsin

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Cite this

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title = "Effect of pressure and solvent dielectric constant on the kinetic constants of trypsin-catalyzed reaction",
abstract = "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 studies 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 rate. Moreover, the decrease of activation volume by lowering the solvent dielectric constant implies a solvent penetration of the active site and a reduction of electrostatic energy for the formation of dipole of the active site oxyanion hole. When the dielectric 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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T1 - Effect of pressure and solvent dielectric constant on the kinetic constants of trypsin-catalyzed reaction

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AU - Chi, Young Min

PY - 2000/2/1

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N2 - 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 studies 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 rate. Moreover, the decrease of activation volume by lowering the solvent dielectric constant implies a solvent penetration of the active site and a reduction of electrostatic energy for the formation of dipole of the active site oxyanion hole. When the dielectric 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.

AB - 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 studies 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 rate. Moreover, the decrease of activation volume by lowering the solvent dielectric constant implies a solvent penetration of the active site and a reduction of electrostatic energy for the formation of dipole of the active site oxyanion hole. When the dielectric 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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