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N ‐acylphosphatidylethanolamine‐hydrolysing phospholipase D lacks the ability to transphosphatidylate
Author(s) -
Petersen Gitte,
Hansen Harald S
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00861-3
Subject(s) - anandamide , phospholipase d , mastoparan , chemistry , biochemistry , enzyme , stereochemistry , cannabinoid receptor , g protein , agonist , receptor
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 2 , 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.