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Circular dichroism changes in galactosyltransferase upon substrate binding;.

C R Geren, S C Magee, K E Ebner

    Biochemistry
    |April 8, 1975
    PubMed
    Summary
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    Circular dichroism reveals that UDP-galactose binding induces a conformational change in bovine galactosyltransferase. This structural shift involves aromatic amino acid residues, impacting enzyme activity.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Galactosyltransferase is crucial for synthesizing complex carbohydrates.
    • Understanding its conformational dynamics is key to elucidating its catalytic mechanism.
    • Bovine skim milk serves as a source for enzyme isolation.

    Purpose of the Study:

    • To investigate the conformational changes in galactosyltransferase upon substrate binding.
    • To determine the role of UDP-galactose in enzyme structure.
    • To explore the specificity of ligand-induced conformational changes.

    Main Methods:

    • Circular dichroism (CD) spectroscopy was employed.
    • Near-ultraviolet CD spectra were analyzed.
    • Studies were conducted on galactosyltransferase isolated from bovine skim milk.

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  • The effects of UDP-galactose, UDP, and glucose on the enzyme-Mn2+ complex were examined.

    • Main Results:

    • UDP-galactose binding caused a decrease in negative ellipticity (205-220 nm) and positive increases (265-290 nm).
    • These spectral changes indicate a conformational alteration involving aromatic amino acid residues.
    • UDP or glucose binding did not induce significant changes in the near-ultraviolet CD spectrum.

    Conclusions:

    • UDP-galactose binding induces a specific conformational change in galactosyltransferase.
    • This conformational change is likely essential for the enzyme's catalytic function.
    • The enzyme's response is specific to the UDP-galactose substrate, not UDP or glucose alone.