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Lactoperoxidase as a potential drug target.

Jörg Flemmig1,2, Jana Gau1, Denise Schlorke1,2

  • 1a Institute for Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Härtelstraße 16 - 18 , 04107 Leipzig , Germany.

Expert Opinion on Therapeutic Targets
|November 13, 2015
PubMed
Summary

Lactoperoxidase (LPO), a mammalian heme peroxidase, aids immune defense by oxidizing thiocyanate and iodide. Specific organic substrates significantly boost LPO's antimicrobial and biotechnological functions.

Keywords:
(pseudo-)halogenating activity3,4-dihydroxylated phenylic compoundsheme peroxidaseshypothiocyaniteinflammationinnate immunitylactoperoxidasemucous surfacesmyeloperoxidaseoxidized iodine species

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Area of Science:

  • Biochemistry
  • Immunology
  • Enzymology

Background:

  • Lactoperoxidase (LPO) is a mammalian heme peroxidase crucial for humoral immune defense.
  • It functions in external secretions, oxidizing thiocyanate and iodide to combat pathogens.
  • LPO's activity is vital for both immune defense and biotechnological applications.

Purpose of the Study:

  • To review current knowledge on LPO's structure, catalytic mechanisms, and generated species.
  • To discuss LPO's redox properties and kinetics, particularly under pathological conditions.
  • To summarize structural insights and substrate interactions influencing LPO activity.

Main Methods:

  • Review of enzymatic structure and catalytic cycles.
  • Analysis of redox properties and kinetic aspects.
  • Summary of crystallographic studies on substrate interactions.

Main Results:

  • LPO generates oxidized thiocyanate and/or iodine species.
  • Substrate binding and oxidation can inhibit or promote LPO activity.
  • Hydrophobic organic substrates with a 3,4-dihydroxyphenyl structure enhance LPO's pseudohalogenating activity.

Conclusions:

  • Strategies to optimize LPO for mucosal defense and biotechnology are discussed.
  • Specific organic substrates offer a novel approach to enhance LPO's antimicrobial efficacy.
  • Enhanced LPO activity through substrate optimization holds promise for therapeutic and industrial uses.