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Related Experiment Videos

Laccases: structure, reactions, distribution.

Harald Claus1

  • 1Institut für Molekulare Biophysik, University of Mainz Jakob-Welder-Weg 26, 55128 Mainz, Germany. hcdclaus@t-online.de

Micron (Oxford, England : 1993)
|March 24, 2004
PubMed
Summary
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Laccases are versatile enzymes that oxidize compounds using oxygen. Recently discovered in prokaryotes, these multi-copper proteins have broad biotechnological potential.

Area of Science:

  • Biochemistry
  • Enzymology
  • Biotechnology

Background:

  • Laccases (EC 1.10.3.2) are multi-copper oxidoreductases utilizing molecular oxygen.
  • They play roles in pathogenicity, immunity, morphogenesis, and the breakdown of complex organic matter like lignin.
  • Their high non-specific oxidation capacity makes them valuable biocatalysts.

Purpose of the Study:

  • To highlight the expanding understanding of laccase distribution.
  • To underscore the significance of bacterial laccases.
  • To position laccases within the broader multi-copper protein family.

Main Methods:

  • Phylogenetic analysis to determine evolutionary relationships.
  • Structural biology to elucidate bacterial laccase characteristics.

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  • Review of existing literature on laccase functions and distribution.

    • Main Results:

    • Laccases are now known to be widespread in prokaryotes, not just eukaryotes.
    • The first crystal structure of a bacterial laccase has been determined.
    • Laccases are phylogenetically linked to other multi-copper proteins like ceruloplasmin.

    Conclusions:

    • The discovery of prokaryotic laccases significantly broadens their known distribution.
    • Bacterial laccases offer new avenues for biotechnological applications.
    • Laccases represent a diverse group within the multi-copper protein superfamily.