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

TY - JOUR

T1 - N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate

AU - Petersen, G.

AU - Hansen, Harald S.

PY - 1999/7/16

Y1 - 1999/7/16

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0033063326&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(99)00861-3

DO - 10.1016/S0014-5793(99)00861-3

M3 - Journal article

AN - SCOPUS:0033063326

SN - 0014-5793

VL - 455

SP - 41

EP - 44

JO - F E B S Letters

JF - F E B S Letters

IS - 1-2

ER -