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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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Defining Substrate Specificities for Lipase and Phospholipase Candidates
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Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders.

Daniel M Lajoie1, Sue A Roberts1, Pamela A Zobel-Thropp2

  • 1From the Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 and.

The Journal of Biological Chemistry
|March 11, 2015
PubMed
Summary
This summary is machine-generated.

Sicariid spider venom phospholipase D toxins target specific lipid substrates. Enzyme variations in headgroup preference, particularly for choline versus ethanolamine, influence venom activity and may explain differences in dermonecrotic potential.

Keywords:
Crystal StructureEnzyme MechanismLoxoscelesLoxoscelismPhospholipase DSicariusSphingomyelinaseSubstrate SpecificityToxin

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Area of Science:

  • Biochemistry
  • Toxicology
  • Structural Biology

Background:

  • Sicariid spider venoms contain phospholipase D (PLD) toxins responsible for severe dermonecrosis.
  • These PLD enzymes hydrolyze sphingolipid and lysolipid substrates, producing cyclic phosphates.
  • Sphingomyelin and lysophosphatidylcholine are considered the most medically significant substrates.

Purpose of the Study:

  • To investigate the substrate specificity of sicariid PLD toxins.
  • To compare the activity of diverse sicariid toxins against various sphingolipid and lysolipid substrates.
  • To understand the structural basis for observed substrate preferences.

Main Methods:

  • Utilized phosphorus-31 Nuclear Magnetic Resonance ((31)P NMR) spectroscopy to assess enzyme activity.
  • Tested three phylogenetically distinct sicariid toxins against a panel of lipid substrates.
  • Determined the crystal structure of a Sicarius terrosus enzyme at 2.1 Å resolution.

Main Results:

  • Two of the three toxins exhibited higher turnover rates for sphingolipids compared to lysolipids.
  • All tested toxins demonstrated a preference for positively charged headgroups (choline/ethanolamine) over neutral ones (glycerol/serine).
  • Significant variation was observed in the preference for choline versus ethanolamine headgroups among the enzymes.

Conclusions:

  • Enzyme substrate specificity, particularly headgroup preference, varies among sicariid PLDs.
  • This variability may contribute to differences in the dermonecrotic potential of various sicariid venoms.
  • Understanding these preferences offers insights into venom evolution and potential interactions with prey lipids.