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Related Experiment Videos

Further electron microscope studies on pyruvate carboxylase

F Mayer, J C Wallace, D B Keech

    European Journal of Biochemistry
    |November 1, 1980
    PubMed
    Summary

    Chicken, sheep, and rat pyruvate carboxylases exhibit a tetrahedron-like structure. This enzyme

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Pyruvate carboxylase is a crucial enzyme in metabolism.
    • Understanding its structure is key to elucidating its function.

    Purpose of the Study:

    • To investigate the fine structure of pyruvate carboxylase from chicken, sheep, and rat.
    • To determine how the enzyme's structure is affected by acetyl-coenzyme A.

    Main Methods:

    • Negative staining electron microscopy
    • Electron microscopic tilting techniques
    • Biophysical modeling experiments

    Main Results:

    • The enzyme presents a tetrahedron-like structure composed of four subunits.
    • In the presence of acetyl-coenzyme A, a compact, triangular form is observed.
    • Absence of acetyl-coenzyme A leads to more open, rhomboid structures, representing flattened forms.
    • Subunits show a cleft, suggesting two distinct domains.

    Conclusions:

    • Pyruvate carboxylase adopts a flexible quaternary structure.
    • Acetyl-coenzyme A influences the enzyme's conformation.
    • The observed cleft indicates potential functional or regulatory domains within subunits.

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