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Extracellular enzymes: gene regulation and structure function relationship studies.

A S Jarnagin, E Ferrari

    Biotechnology (Reading, Mass.)
    |January 1, 1992
    PubMed
    Summary
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    Subtilisin BPN' mutations rarely alter overall structure, showing high tolerance. However, these mutations significantly impact enzyme function, including catalytic efficiency and stability.

    Area of Science:

    • Enzymology
    • Protein Engineering
    • Structural Biology

    Background:

    • Subtilisin BPN' exhibits remarkable tolerance to single and multiple mutations, preserving overall structural integrity.
    • High sequence homology and structural similarity exist among subtilisin family enzymes, such as subtilisin Carlsberg, proteinase K, and thermitase, despite sequence variations.

    Purpose of the Study:

    • To investigate the structural and functional consequences of mutations in subtilisin BPN'.
    • To understand the molecular basis of enzyme adaptation and evolution through mutation analysis.

    Main Methods:

    • Comparative structural analysis of subtilisin BPN' and related enzymes using techniques like alpha-carbon superposition.
    • Evaluation of the impact of mutations on enzyme properties such as catalytic efficiency, substrate preference, and stability.

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    Main Results:

    • Most single mutations in subtilisin BPN' do not cause significant global structural changes.
    • Despite structural stability, mutations can profoundly affect enzyme activity, substrate specificity, and stability.
    • Structural analysis of mutants provides atomic-level insights into mutation effects.

    Conclusions:

    • Subtilisin's structure is robust, allowing for sequence variation while maintaining overall form.
    • Mutations are key drivers of functional diversification in subtilisins.
    • Understanding mutation-induced structural changes aids in predicting and engineering enzyme properties.