PMID- 10526230
OWN - NLM
STAT- MEDLINE
DCOM- 19991202
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1441
IP  - 1
DP  - 1999 Oct 18
TI  - Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression
      and site-directed mutagenesis(1).
PG  - 77-84
AB  - Anandamide (arachidonoylethanolamide) is an endogenous ligand for cannabinoid
      receptors, and its cannabimimetic activities are lost when the compound is
      hydrolyzed to arachidonic acid and ethanolamine by an enzyme referred to as
      anandamide amidohydrolase. We cloned a cDNA for the enzyme of porcine brain, and 
      the cDNA encoded a protein of 579 amino acids with a molecular mass of 62.9 kDa. 
      The amino acid sequence was 81, 80 and 85% identical with the enzymes previously 
      cloned from the liver of rat, mouse, and human, respectively. When the enzyme
      protein was overexpressed in COS-7 cells, the particulate fraction of the cells
      showed an anandamide hydrolyzing activity and also catalyzed the reverse reaction
      synthesizing anandamide from arachidonic acid and ethanolamine both with a
      specific activity of 0. 2-0.3 micromol/min/mg protein at 37 degrees C. The brain 
      enzyme exhibited a wide substrate specificity hydrolyzing oleamide,
      2-arachidonoylglycerol, and methyl arachidonate. The point mutation of Ser-217,
      Asp-237, Ser-241, or Cys-249 completely abolished the hydrolyses of all the
      above-mentioned substrates as well as the synthesis of anandamide in the reverse 
      reaction.
FAU - Goparaju, S K
AU  - Goparaju SK
AD  - Department of Biochemistry, Tokushima University, School of Medicine,
      Kuramoto-cho, Tokushima, Japan.
FAU - Kurahashi, Y
AU  - Kurahashi Y
FAU - Suzuki, H
AU  - Suzuki H
FAU - Ueda, N
AU  - Ueda N
FAU - Yamamoto, S
AU  - Yamamoto S
LA  - eng
SI  - GENBANK/AB027132
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (DNA, Complementary)
RN  - EC 3.5.- (Amidohydrolases)
RN  - EC 3.5.1.- (fatty-acid amide hydrolase)
SB  - IM
MH  - Amidohydrolases/biosynthesis/chemistry/*genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/*enzymology
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Cloning, Molecular
MH  - DNA, Complementary/chemistry
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Sequence Alignment
MH  - Substrate Specificity
MH  - Swine
EDAT- 1999/10/20 00:00
MHDA- 1999/10/20 00:01
CRDT- 1999/10/20 00:00
PHST- 1999/10/20 00:00 [pubmed]
PHST- 1999/10/20 00:01 [medline]
PHST- 1999/10/20 00:00 [entrez]
AID - S1388198199001432 [pii]
AID - 10.1016/s1388-1981(99)00143-2 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Oct 18;1441(1):77-84. doi:
      10.1016/s1388-1981(99)00143-2.