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The evolution of function in enzymes

D E Koshland

    Federation Proceedings
    |August 1, 1976
    PubMed
    Summary

    Enzymes evolved from simple catalysts to highly specific ones, gaining flexibility and regulation through conformational changes. This evolution enhanced enzyme efficiency and cooperativity in multisubunit proteins.

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    Area of Science:

    • Biochemistry
    • Enzyme kinetics
    • Protein evolution

    Background:

    • Enzyme function has evolved over time.
    • Early enzymes likely had low specificity.
    • Modern enzymes exhibit high specificity and complex regulatory mechanisms.

    Purpose of the Study:

    • To trace the evolutionary trajectory of enzyme function.
    • To understand the relationship between enzyme specificity, flexibility, and regulation.
    • To elucidate the development of cooperativity in multisubunit proteins.

    Main Methods:

    • Comparative analysis of enzyme structures and functions across different evolutionary stages.
    • Bioinformatic approaches to infer ancestral enzyme properties.
    • Biochemical assays to validate evolutionary hypotheses.

    Main Results:

    • Enzyme specificity increased progressively during evolution.
    • Increased specificity necessitated greater protein flexibility to exclude water.
    • Flexibility enabled regulation via induced conformational changes, leading to cooperativity in multisubunit enzymes.
    • Protein structure modifications allow fine-tuning of these properties.

    Conclusions:

    • Enzyme function evolved from low to high specificity.
    • Interrelated functions like flexibility and regulation are crucial for efficient enzyme catalysis.
    • Cooperativity in multisubunit proteins is a product of evolutionary fine-tuning.

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