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Related Experiment Videos

Superefficient enzymes.

M E Stroppolo1, M Falconi, A M Caccuri

  • 1INFM and Department of Biology, University of Rome Tor Vergata, Rome, Italy.

Cellular and Molecular Life Sciences : CMLS
|November 6, 2001
PubMed
Summary
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Diffusion-controlled enzymes achieve maximal reaction rates limited only by substrate diffusion. These "perfect" enzymes, like triose phosphate isomerase, utilize facilitated encounters for rapid association, showcasing efficient biological catalysis.

Area of Science:

  • Biochemistry
  • Enzymology
  • Chemical Kinetics

Background:

  • Diffusion-controlled enzymes exhibit second-order rate constants between 10(8)-10(10) M(-1)s(-1).
  • These rates approach the theoretical maximum for bimolecular reactions in solution.
  • Such enzymes are termed "perfect" as their rate-limiting step is diffusion, not chemical transformation.

Purpose of the Study:

  • To review enzymes with very fast second-order rate constants.
  • To highlight enzymes where substrate diffusion is the rate-limiting step.
  • To examine triose phosphate isomerase and Cu,Zn superoxide dismutase as examples.

Main Methods:

  • Review of existing literature on diffusion-controlled enzymes.
  • Analysis of kinetic data for specific enzyme examples.

Related Experiment Videos

  • Discussion of theoretical predictions for bimolecular reactions.

    • Main Results:

    • Identified enzymes with exceptionally high second-order rate constants.
    • Described mechanisms facilitating enzyme-substrate encounters, including electric fields and dimensionality reduction.
    • Presented triose phosphate isomerase and Cu,Zn superoxide dismutase as case studies.

    Conclusions:

    • Diffusion-controlled enzymes represent highly optimized biological catalysts.
    • Facilitated diffusion significantly enhances enzyme-substrate association rates.
    • These enzymes demonstrate the efficiency of diffusion as a rate-limiting factor in biological systems.