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Linoleate diol synthase related enzymes of the human pathogens Histoplasma capsulatum and Blastomyces dermatitidis

Ernst H Oliw1

  • 1Division of Biochemical Pharmacology, Department of Pharmaceutical Biosciences, Uppsala University, Box 591, SE 751 24, Uppsala, Sweden.

Archives of Biochemistry and Biophysics
|November 15, 2020
PubMed

Insights

Researchers discovered a novel epoxy alcohol synthase (EAS) in human pathogens Histoplasma capsulatum and Blastomyces dermatitidis. This enzyme transforms specific hydroperoxides, offering new insights into fungal metabolism and potential therapeutic targets.

Area of Science:

  • Medical Mycology
  • Enzymology
  • Biochemistry

Background:

  • Histoplasma capsulatum is a significant human lung pathogen.
  • H. capsulatum belongs to the Ajellomycetaceae family, alongside other fungal pathogens.
  • Fungal pathogens possess enzymes with dioxygenase (DOX) and cytochrome P450 domains, including the linoleate diol synthase (LDS) family.

Purpose of the Study:

  • To investigate the function of specific enzyme groups within H. capsulatum and B. dermatitidis.
  • To characterize the enzymatic activities of novel enzymes identified in these human fungal pathogens.
  • To determine the substrate specificity and products of these enzymes in relation to fatty acid oxidation.

Main Methods:

  • Genome analysis to identify enzyme families.
  • Gene expression in relevant fungal species.
  • Enzymatic assays using various hydroperoxides of linoleic and alpha-linolenic acids.
  • Analysis of reaction products using chromatographic and spectroscopic methods.

Main Results:

  • Identified three homologous enzyme groups in H. capsulatum and B. dermatitidis genomes.
  • One enzyme group showed 10R-DOX activity in B. dermatitidis.
  • A novel epoxy alcohol synthase (EAS) was identified in both species, efficiently converting 13S-hydroperoxy-9Z,11E-octadecadienoic acid to 12(13S)epoxy-11-hydroperoxy-9Z-octadecenoic acid.

Conclusions:

  • A novel EAS enzyme has been identified in Histoplasma capsulatum and Blastomyces dermatitidis.
  • The likely physiological substrate for this novel EAS is 13S-hydroperoxy-9Z,11E-octadecadienoic acid.
  • This finding contributes to understanding the metabolic pathways of these important fungal pathogens.
Keywords:
Cytochrome P450Linoleate diol synthaseLipid metabolismMass spectrometryOxygenation mechanismParacoccidioides brasiliensis

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