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Evolution in the structure and function of aspartic proteases.

J Tang, R N Wong

    Journal of Cellular Biochemistry
    |January 1, 1987
    PubMed
    Summary
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    Aspartic proteases function in acidic environments and are synthesized as inactive zymogens. This review summarizes structure-function models for aspartic proteases and their zymogens, highlighting recent findings.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Molecular Biology

    Background:

    • Aspartic proteases (EC3.4.23) are a distinct enzyme family functioning optimally in acidic conditions.
    • Their acidic environment requirement limits their distribution compared to other proteases like serine proteases.
    • Key sources include mammalian stomachs, lysosomes, kidneys, yeast, and fungi.

    Purpose of the Study:

    • To review major structure-function models of aspartic proteases.
    • To emphasize recent findings in aspartic protease research.
    • To correlate models across different aspartic proteases, including fungal and mammalian types.

    Main Methods:

    • Literature review of existing studies on aspartic proteases.
    • Analysis of structure-function relationships.

    Related Experiment Videos

  • Comparison of models for various aspartic proteases and their zymogens.

    • Main Results:

    • Mammalian aspartic proteases are synthesized as zymogens and activated.
    • Evidence suggests fungal aspartic proteases may also be synthesized as zymogens.
    • Structure-function models provide insights into enzyme mechanisms.

    Conclusions:

    • Aspartic proteases exhibit conserved catalytic mechanisms despite diverse sources.
    • Understanding zymogen activation is crucial for comprehending aspartic protease function.
    • Further research can unify structure-function models across the aspartic protease family.