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

G. Petersen, Harald S. Hansen

    66 Citations (Scopus)

    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 (=100 µM) while PMSF in high concentrations (10 mM) tends to stabilise NAPE-PLD activity. Oleate inhibits NAPE-PLD but the enzyme is not affected by PIP, a-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. Copyright (C) 1999 Federation of European Biochemical Societies.
    Original languageEnglish
    JournalF E B S Letters
    Volume455
    Issue number1-2
    Pages (from-to)41-44
    Number of pages4
    ISSN0014-5793
    DOIs
    Publication statusPublished - 16 Jul 1999

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