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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

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Phosphatidate phosphatase of dermatophytes

C Kasinathan1, A Chopra1, G K Khuller1

  • 1Department of Biochemistry, Postgraduate Institute of Medical Education and Research, 160 012, Chandigarh, India.

Lipids
|August 14, 2016
PubMed

Insights

Phosphatidate phosphatase activity was found in pathogenic fungi Microsporum gypseum and Epidermophyton floccosum. Enzyme activity was pH 6.0-dependent and sensitive to metal ions and phospholipids.

Area of Science:

  • Biochemistry
  • Mycology
  • Enzymology

Background:

  • Pathogenic fungi, including dermatophytes, possess enzymes crucial for their survival and virulence.
  • Phosphatidate phosphatase (EC 3.1.3.4) plays a key role in lipid metabolism.

Purpose of the Study:

  • To characterize phosphatidate phosphatase in filamentous pathogenic fungi, specifically Microsporum gypseum and Epidermophyton floccosum.
  • To investigate the subcellular localization, optimal pH, and sensitivity to inhibitors of this enzyme.

Main Methods:

  • Enzyme assays were performed on mitochondrial and microsomal fractions of M. gypseum and E. floccosum.
  • The effects of various metal ions (Fe2+, Mn2+, Cu2+, Ba2+, Hg2+, Mg2+), sulfhydryl reagents, and phospholipids (phosphorylcholine, lysophosphatidylcholine, phosphatidylcholine) on enzyme activity were assessed.

Main Results:

  • Phosphatidate phosphatase was detected in both mitochondrial and microsomal fractions of both fungal species, with a pH optimum of 6.0.
  • The enzyme from E. floccosum was more active than that from M. gypseum.
  • Both enzymes were inhibited by several divalent metal ions, with the E. floccosum microsomal enzyme showing complete inhibition by Mn2+ and Fe2+. Mg2+ dependency was observed in the presence of EDTA.
  • Sulfhydryl reagents did not inhibit the enzyme. Phosphorylcholine and lysophosphatidylcholine caused significant inhibition, while phosphatidylcholine showed less inhibition.

Conclusions:

  • Phosphatidate phosphatase is present in pathogenic dermatophytes and exhibits distinct properties in different subcellular fractions and species.
  • The enzyme's sensitivity to specific metal ions and phospholipids suggests potential regulatory mechanisms and targets for antifungal strategies.

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