N‐acylphosphatidylethanolamine‐hydrolysing phospholipase D lacks the ability to transphosphatidylate
Open Access
- 15 July 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 455 (1-2) , 41-44
- https://doi.org/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 (≥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 PIP2, α‐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.Keywords
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