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

Petersen, G & Hansen, HS 1999, 'N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate', F E B S Letters, vol. 455, no. 1-2, pp. 41-44. https://doi.org/10.1016/S0014-5793(99)00861-3

APA

Petersen, G., & Hansen, H. S. (1999). N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate. F E B S Letters, 455(1-2), 41-44. https://doi.org/10.1016/S0014-5793(99)00861-3

Vancouver

Petersen G, Hansen HS. N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate. F E B S Letters. 1999 Jul 16;455(1-2):41-44. https://doi.org/10.1016/S0014-5793(99)00861-3

Author

Petersen, G. ; Hansen, Harald S. / N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate. In: F E B S Letters. 1999 ; Vol. 455, No. 1-2. pp. 41-44.

Bibtex

@article{7e642516b0a440cabe82521eec82add6,
title = "N-acylphosphatidylethanolamine-hydrolysing phospholipase D lacks the ability to transphosphatidylate",
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.",
author = "G. Petersen and Hansen, {Harald S.}",
year = "1999",
month = jul,
day = "16",
doi = "10.1016/S0014-5793(99)00861-3",
language = "English",
volume = "455",
pages = "41--44",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-2",

}

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