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April 1, 1985Proceedings of the National Academy of Sciences195 citationsOpen Access

Alternative view of enzyme reactions.

MDMichael J. S. DewarDSDonn M. Storch

Key Points

  • To re-evaluate enzyme reactions by considering the absence of solvent and its effects on reaction kinetics.
  • Proposes that enzyme-substrate interactions occur without solvent interference.
  • Discusses previous findings on gas phase ionic reactions compared to those in solution.
  • Analyzes peptide cleavage by chymotrypsin and carboxypeptidase A under this new perspective.
  • Suggests that enzyme specificity and reaction rates are enhanced without solvent.
  • Findings indicate alternative interpretations align better with gas phase reaction behavior.
  • Challenges traditional views based on solution chemistry.

Abstract

Since adsorption of the substrate in the active site of an enzyme can occur only if all solvent is squeezed out from between them, any reaction between them takes place in the absence of any intervening solvent--i.e., as it would in the gas phase. Recent work has shown that ionic reactions in the gas phase often differ greatly from analogous processes in solution. Therefore, current interpretations of enzyme reactions in terms of solution chemistry are misguided. The large rates and specificity of enzyme reactions may be due simply to elimination of the solvent. The cleavage of peptides by chymotrypsin and carboxypeptidase A can be interpreted satisfactorily in this way.

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Cite This Study

Dewar et al. (1985) studied this question.

synapsesocial.com/papers/6a19c46f05af093a17f6893fhttps://doi.org/10.1073/pnas.82.8.2225
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