Abstract
Anandamide (arachidonylethanolamide) loses its cannabimimetic activities when it is enzymatically hydrolyzed to arachidonic acid and ethanolamine.si1 The enzyme responsible for the hydrolysis will be referred to as “anandamide amidohydrolase” or just “hydrolase” in this article. Previously we partially purified this enzyme from the microsomes of porcine brain, and showed that the same enzyme preparation catalyzed not only the anandamide hydrolysis but also its synthesis by the reverse reaction.2 We examined various inhibitors (arachidonyl trifluoromethyl ketone, p-chloromercuribenzoic acid, phenylmethylsulfonyl fluoride and diisopropyl fluorophosphate) which inhibited the hydrolase and synthase activities in parallel. Together with several other lines of enzymological evidence, it was suggested that the two enzyme activities are attributable to a single enzyme protein.2
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Ueda, N. et al. (1999). Enzymological and Molecular Biological Studies on Anandamide Amidohydrolase. In: Honn, K.V., Marnett, L.J., Nigam, S., Dennis, E.A. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury, 4. Advances in Experimental Medicine and Biology, vol 469. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4793-8_75
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DOI: https://doi.org/10.1007/978-1-4615-4793-8_75
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