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Cofactor processing in galactose oxidase.

S J Firbank1, M Rogers, R Hurtado-Guerrero

  • 1Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

Biochemical Society Transactions
|May 30, 2003
PubMed
Summary
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Galactose oxidase (GO) biogenesis involves copper and oxygen-dependent cofactor formation. The pro-peptide acts as a chaperone, guiding copper binding and cofactor maturation, though its cleavage mechanism remains unknown.

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Chemistry

Background:

  • Galactose oxidase (GO) is a copper-containing enzyme crucial for catalyzing galactose oxidation.
  • Its catalytic mechanism and activation involve a radical cofactor derived from Tyr-272.
  • Cofactor biogenesis requires post-translational, autocatalytic thioether cross-linking between Cys-228 and Tyr-272, linked to pro-peptide cleavage.

Purpose of the Study:

  • To investigate the role of the pro-peptide in galactose oxidase maturation.
  • To elucidate the autocatalytic process of mature GO formation from its pro-enzyme.
  • To compare the structures of pro-GO and mature GO to understand the pro-peptide's function.

Main Methods:

  • Purification of pro-enzyme under copper-free conditions.

Related Experiment Videos

  • Autocatalytic maturation of GO upon addition of copper and oxygen.
  • Structural comparison of pro-GO and mature GO using X-ray crystallography or similar techniques.

    • Main Results:

    • Mature oxidized GO can be formed autocatalytically from pro-GO with copper and oxygen.
    • Structural analysis reveals overall similarity between pro-GO and mature GO.
    • Significant local differences in main chain and side chain positions exist, particularly in the active site, suggesting a chaperone role for the pro-peptide.

    Conclusions:

    • The pro-peptide of galactose oxidase likely functions as an intramolecular chaperone.
    • It facilitates an open active-site structure for copper binding and cofactor formation.
    • The precise mechanism of pro-peptide cleavage during GO maturation remains undetermined.