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Temperature: a "shaping force' in protein evolution

G N Somero, P S Low

    Biochemical Society Symposium
    |January 1, 1976
    PubMed
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    Enzyme function is conserved across temperatures, with catalytic efficiency adapting to environmental conditions. This involves a trade-off between thermal stability and optimal enzyme performance.

    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Protein adaptation

    Background:

    • Enzymes from different species exhibit conserved ligand-binding affinities despite varying adaptation temperatures.
    • Enzyme regulation relies on maintaining a balance between ligand-binding ability and intracellular ligand concentrations.

    Purpose of the Study:

    • To investigate how homologous enzymes adapt to different temperatures.
    • To understand the relationship between enzyme structure, function, and thermal adaptation.
    • To explore the mechanisms behind temperature compensation in enzyme catalysis and ligand binding.

    Main Methods:

    • Comparative analysis of homologous enzymes from species with diverse temperature adaptations.
    • Examination of enzyme kinetics, including activation free energies, enthalpy, and entropy.

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  • Correlation of enzyme properties with adaptation temperatures and thermal stability.

    • Main Results:

    • Ligand-binding affinities are conserved across homologous enzymes adapted to different temperatures.
    • Enzyme catalytic efficiencies show temperature-compensatory differences, with low-temperature enzymes having higher turnover rates.
    • Activation free energies correlate with adaptation temperature, influenced by changes in weak bond formation/rupture during catalysis.
    • Thermal stability in warm-adapted enzymes may compromise catalytic efficiency, indicating an adaptational trade-off.

    Conclusions:

    • Enzyme regulation necessitates conserved ligand-binding affinities, irrespective of adaptation temperature.
    • Temperature adaptation in enzymes involves compensatory changes in catalytic efficiency, often linked to alterations in conformational dynamics and weak bond interactions.
    • A compromise exists between achieving high thermal stability and optimal catalytic efficiency in enzymes, shaping their adaptive strategies.