1: Biochem J.  2004 Apr 1;379(Pt 1):99-106.  

N-cyclohexanecarbonylpentadecylamine: a selective inhibitor of the acid amidase
hydrolysing N-acylethanolamines, as a tool to distinguish acid amidase from
fatty acid amide hydrolase.

Tsuboi K, Hilligsmann C, Vandevoorde S, Lambert DM, Ueda N.

Department of Biochemistry, Kagawa University School of Medicine, 1750-1
Ikenobe, Miki, Kagawa 761-0793, Japan.

Anandamide ( N-arachidonoylethanolamine) and other bioactive N-acylethanolamines
are degraded to their corresponding fatty acids and ethanolamine. This
hydrolysis is mostly attributed to catalysis by FAAH (fatty acid amide
hydrolase), which exhibits an alkaline pH optimum. In addition, we have
identified another amidase which catalyses the same reaction exclusively at
acidic pH values [Ueda, Yamanaka and Yamamoto (2001) J. Biol. Chem. 276,
35552-35557]. In attempts to find selective inhibitors of this acid amidase, we
screened various derivatives of palmitic acid, 1-hexadecanol, and
1-pentadecylamine with N-palmitoylethanolamine as substrate. Here we show that
N-cyclohexanecarbonylpentadecylamine inhibits the acid amidase from rat lung
with an IC50 of 4.5 microM, without inhibiting FAAH at concentrations up to 100
microM. The inhibition was reversible and non-competitive. This compound also
inhibited the acid amidase in intact alveolar macrophages. With the aid of this
inhibitor, it was revealed that rat basophilic leukaemia cells possess the acid
amidase as well as FAAH. Thus the inhibitor may be a useful tool to distinguish
the acid amidase from FAAH in various tissues and cells and to elucidate the
physiological role of the enzyme.

PMID: 14686878 [PubMed - in process]