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

Petersen G, Hansen HS
FEBS Lett. 1999 455 (1-2): 41-4

PMID: 10428468 · DOI:10.1016/s0014-5793(99)00861-3

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 (> or = 100 microM) 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, alpha-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.

MeSH Terms (11)

Animals Detergents Enzyme Inhibitors Hydrolysis Kinetics Octoxynol Phosphatidic Acids Phosphatidylethanolamines Phospholipase D Rats Rats, Sprague-Dawley

Connections (1)

This publication is referenced by other Labnodes entities:

Links