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Evolutionary dynamics of enzymes

L Demetrius1

  • 1Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138, USA.

Protein Engineering
|August 1, 1995
PubMed
Summary
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Enzymes evolve through mutation and selection, leading to diverse reaction rates and substrate specificities. This model classifies enzymes into three types, predicting evolutionary trends and linking structural properties to function.

Area of Science:

  • Biochemistry and Molecular Biology
  • Evolutionary Biology
  • Enzyme Kinetics

Background:

  • Enzymes exhibit a wide range of reaction rates and substrate specificities.
  • These kinetic properties are influenced by evolutionary pressures.
  • Primordial enzymes likely possessed poor catalytic activity and broad substrate specificity.

Purpose of the Study:

  • To develop a model explaining enzyme diversity based on evolutionary forces.
  • To classify enzymes using thermodynamic parameters (activation enthalpy and entropy).
  • To predict evolutionary trends in enzyme reaction rates and substrate specificity.

Main Methods:

  • Classified enzymes into three types based on thermodynamic parameters: Type 1 (ΔH* > 0, ΔS* < 0), Type 2 (ΔH* ≤ 0, ΔS* ≤ 0), and Type 3 (ΔH* > 0, ΔS* > 0).

Related Experiment Videos

  • Studied evolutionary dynamics under mutation and selection acting on genes and organisms.
  • Analyzed predicted evolutionary trends for reaction rate and binding specificity for each enzyme type.

    • Main Results:

    • Type 1 enzymes show random changes in rate and specificity.
    • Type 2 and Type 3 enzymes exhibit unidirectional increases in rate and specificity.
    • Type 2 and Type 3a enzymes achieve diffusion-controlled rates with absolute specificity; Type 3b shows non-diffusion-controlled rates with absolute specificity.
    • Enzymes with diffusion-controlled rates possess absolute substrate specificity and represent a small subset of all enzymes.

    Conclusions:

    • The evolutionary model successfully codifies the diversity of present-day enzyme functional properties.
    • Enzyme structural properties (thermodynamic parameters) are linked to functional properties (rate and specificity).
    • A general relationship exists: diffusion-controlled rates correlate with absolute substrate specificity.