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Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
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Laccase: enzyme revisited and function redefined.

Krishna Kant Sharma1, Ramesh Chander Kuhad

  • 1Lignocellulose Biotechnology Laboratory, Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110 021 India.

Indian Journal of Microbiology
|October 27, 2012
PubMed
Summary
This summary is machine-generated.

Enzymes can have multiple roles beyond their primary function, a phenomenon known as protein moonlighting. Laccases, traditionally found in eukaryotes, are now recognized in prokaryotes, showcasing diverse physiological functions.

Keywords:
IsozymeLaccaseLignificationMoonlightOxidoreductase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • The traditional view posits one enzyme per physiological role.
  • Protein moonlighting, where a single protein performs multiple functions, is increasingly recognized.
  • Laccases, a type of multi-copper oxidase, were previously primarily identified in eukaryotes.

Purpose of the Study:

  • To explore the concept of protein moonlighting using laccases as a model.
  • To investigate the presence and functions of laccases in prokaryotes.
  • To highlight the plasticity of laccase structure and its implications for multifunctional activity.

Main Methods:

  • Literature review of existing studies on laccase structure and function.
  • Comparative analysis of laccase roles across different biological kingdoms (eukaryotes and prokaryotes).

Main Results:

  • Laccases exhibit moonlighting behavior, possessing functions beyond their primary catalytic activity.
  • Evidence suggests the existence of laccases in prokaryotes, expanding their known distribution.
  • Laccase structure reveals plasticity with multiple binding sites, supporting multifunctional roles.
  • Specific roles identified: lignin biosynthesis (plants), lignin degradation and melanin synthesis (fungi), and endospore coat protein synthesis (bacteria).

Conclusions:

  • Laccases exemplify moonlighting proteins, challenging the 'one gene-one function' paradigm.
  • The multifunctional nature of laccases allows organisms to adapt to physiological and pathological changes.
  • The discovery of prokaryotic laccases broadens our understanding of enzyme diversity and function.