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Related Experiment Videos

Circular dichroism changes in adenosine deaminase upon substrate analog binding

A Lucacchini, C Bertucci, G Ronca

    The Italian Journal of Biochemistry
    |March 1, 1982
    PubMed
    Summary

    Circular dichroism reveals that purine riboside binding induces a conformational change in adenosine deaminase. This enzyme modification involves aromatic amino acid residues in the active site.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Structural Biology

    Background:

    • Adenosine deaminase (ADA) is a crucial enzyme in purine metabolism.
    • Understanding ADA's mechanism is vital for therapeutic target identification.

    Purpose of the Study:

    • To investigate the conformational changes in adenosine deaminase upon binding of a competitive inhibitor.
    • To elucidate the role of aromatic residues in enzyme-inhibitor interactions.

    Main Methods:

    • Circular dichroism (CD) spectroscopy was employed to study enzyme structure.
    • Adenosine deaminase from calf intestinal mucosa was used.
    • Purine riboside, a competitive inhibitor, was added to the enzyme solution.

    Main Results:

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    • CD spectra showed no significant change in mean residue ellipticity between 250-185 nm.
    • A marked increase in ellipticity was observed in the 300-250 nm region upon inhibitor binding.
    • These spectral changes indicate alterations in the microenvironment of aromatic amino acid residues.

    Conclusions:

    • Purine riboside binding induces a conformational shift in adenosine deaminase.
    • Aromatic amino acid residues are involved in the conformational change upon inhibitor binding.
    • The study provides insights into the allosteric regulation of adenosine deaminase activity.