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Evolution in the structure and function of carboxyl proteases.

J Tang

    Molecular and Cellular Biochemistry
    |July 31, 1979
    PubMed
    Summary
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    Structural analysis reveals carboxyl proteases share homologous structures, suggesting gene duplication and fusion created their complex four-unit design. Cathepsin D

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Extracellular carboxyl (acid) proteases are crucial enzymes with conserved structures.
    • Understanding their structure-function relationship is key to their biological roles.

    Purpose of the Study:

    • To establish a structural and functional model for extracellular carboxyl proteases.
    • To compare the structures of extracellular carboxyl proteases with intracellular counterparts like cathepsin D.

    Main Methods:

    • Analysis of three amino acid sequences.
    • Examination of four crystal structures of carboxyl proteases.

    Main Results:

    • Extracellular gastric and fungal carboxyl proteases exhibit high homology in primary and tertiary structures.

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  • A conserved binding cleft accommodates substrates, with active sites involving Asp-215, Asp-32, and Ser-35.
  • Cathepsin D shares homology but possesses a unique C-terminal hydrophobic tail and larger precursor size.

    • Conclusions:

    • Carboxyl proteases possess a symmetrical, two-lobed structure, likely arising from gene duplication and fusion of four ancestral units.
    • Gene fusion events likely explain the formation of zymogens and the cathepsin D tail.
    • Cathepsin D may represent an evolutionary precursor to gastric carboxyl proteases.