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Manganese lipoxygenase. Purification and characterization

C Su1, E H Oliw

  • 1Division of Biochemical Pharmacology, Department of Pharmaceutical Biosciences, Uppsala Biomedical Center, Uppsala University, S-751 24 Uppsala, Sweden.

The Journal of Biological Chemistry
|May 28, 1998
PubMed
Summary

This study purified a novel manganese-containing linoleic acid (13R)-lipoxygenase from the take-all fungus. The secreted enzyme produces a specific hydroperoxy fatty acid, distinguishing it from known lipoxygenases.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Mycology

Background:

  • Lipoxygenases are crucial enzymes involved in fatty acid metabolism.
  • Understanding fungal lipoxygenases is important for their role in plant-pathogen interactions.

Purpose of the Study:

  • To purify and characterize a novel lipoxygenase from Gäumannomyces graminis.
  • To determine the enzyme's substrate specificity, products, and unique properties.

Main Methods:

  • Purification using chromatography techniques (hydrophobic interaction, cation exchange, lectin affinity, size-exclusion).
  • Enzyme characterization via SDS-PAGE, gel filtration, spectroscopy, and kinetic analysis.
  • Product identification using mass spectrometry and chiral HPLC.

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Main Results:

  • A homogeneous manganese-containing linoleic acid (13R)-lipoxygenase was isolated.
  • The enzyme exhibits optimal activity at pH 7.0 and is heat-stable.
  • It specifically oxygenates linoleic and linolenic acids, producing (13R)-hydroperoxy fatty acids.

Conclusions:

  • The purified enzyme is a novel secreted lipoxygenase with unique characteristics.
  • It differs from known lipoxygenases in its secretion, manganese content, and stereospecific product formation.
  • This finding advances the understanding of fungal enzymes in fatty acid oxidation.