N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate

FEBS Lett. 1999 Jul 16;455(1-2):41-4. doi: 10.1016/s0014-5793(99)00861-3.

Abstract

The N-acylphosphatidylethanolamine-hydrolysing phospholipase D (NAPE-PLD) generates N-acylethanolamines, including N-arachidonoyl-ethanolamine (anandamide), that may be neuroprotective and analgesic. The properties of NAPE-PLD from rat heart and brain microsomes are investigated and compared to those of other PLDs. NAPE-PLD is inhibited by the fatty acid aminohydrolase inhibitor MAFP in high concentrations (> or = 100 microM) while PMSF in high concentrations (10 mM) tends to stabilise NAPE-PLD activity. Oleate inhibits NAPE-PLD but the enzyme is not affected by PIP2, alpha-synuclein or mastoparan. Furthermore, it is for the first time reported that NAPE-PLD is not capable of catalysing a transphosphatidylation reaction like most other known PLDs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Detergents
  • Enzyme Inhibitors / pharmacology
  • Hydrolysis
  • Kinetics
  • Octoxynol
  • Phosphatidic Acids / metabolism*
  • Phosphatidylethanolamines / metabolism*
  • Phospholipase D / antagonists & inhibitors
  • Phospholipase D / metabolism*
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Detergents
  • Enzyme Inhibitors
  • Phosphatidic Acids
  • Phosphatidylethanolamines
  • Octoxynol
  • Phospholipase D