N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate. / Petersen, G.; Hansen, Harald S.
In: F E B S Letters, Vol. 455, No. 1-2, 16.07.1999, p. 41-44.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
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
VL - 455
SP - 41
EP - 44
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 1-2
ER -
ID: 45562586