3.5.1.99: fatty acid amide hydrolase
This is an abbreviated version!
For detailed information about fatty acid amide hydrolase, go to the full flat file.
Word Map on EC 3.5.1.99
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3.5.1.99
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endocannabinoids
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cannabinoids
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pain
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lipase
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agonist
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monoacylglycerol
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2-arachidonoylglycerol
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anxiety
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analgesic
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cannabis
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n-acylethanolamines
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vanilloid
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2-arachidonoyl
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ethanolamide
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palmitoylethanolamide
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carbamate
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rimonabant
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hyperalgesia
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reward
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tone
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nociceptive
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cannabimimetic
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n-arachidonoylethanolamine
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marijuana
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anxiolytic
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nape-pld
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antinociceptive
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oleoylethanolamide
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emotional
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neuropathic
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delta9-tetrahydrocannabinol
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amidase
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amygdalar
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medicine
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catalepsy
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pharmacology
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anti-allodynic
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anxiolytic-like
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monoglyceride
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cannabidiol
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psychoactive
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sleep-inducing
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phytocannabinoids
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anxiety-like
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arachidonyl
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monoacyl
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capsazepine
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aversive
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tetrahydrocannabinol
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drug development
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anti-hyperalgesic
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neuromodulatory
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fluorophosphonate
- 3.5.1.99
-
endocannabinoids
- cannabinoids
- pain
- lipase
- agonist
- monoacylglycerol
- 2-arachidonoylglycerol
-
anxiety
-
analgesic
- cannabis
- n-acylethanolamines
-
vanilloid
-
2-arachidonoyl
- ethanolamide
- palmitoylethanolamide
- carbamate
-
rimonabant
- hyperalgesia
-
reward
-
tone
-
nociceptive
-
cannabimimetic
- n-arachidonoylethanolamine
- marijuana
-
anxiolytic
- nape-pld
-
antinociceptive
- oleoylethanolamide
-
emotional
-
neuropathic
- delta9-tetrahydrocannabinol
- amidase
-
amygdalar
- medicine
- catalepsy
- pharmacology
-
anti-allodynic
-
anxiolytic-like
- monoglyceride
- cannabidiol
-
psychoactive
-
sleep-inducing
-
phytocannabinoids
-
anxiety-like
-
arachidonyl
-
monoacyl
-
capsazepine
-
aversive
- tetrahydrocannabinol
- drug development
-
anti-hyperalgesic
-
neuromodulatory
- fluorophosphonate
Reaction
Synonyms
AAH, anandamide amidohydrolase, AtFAAH, endocannabinoid-degrading enzyme, FA amide hydrolase, FAAH, FAAH-1, FAAH-2, fatty acid amide hydrolase, fatty-acid amide hydrolase, hFAAH, oleamide hydrolase
ECTree
3.5.1.99 fatty acid amide hydrolaseAdvanced search results
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results (Subunits
Subunits on EC 3.5.1.99 - fatty acid amide hydrolase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
oligomer
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wild-type FAAH behaves as a larger oligomer than FAAH protein lacking the N-terminal transmembrane domain. Presence of SDS-resistant oligomers for wild-type FAAH, but not for FAAH protein lacking the N-terminal transmembrane domain. Self-association through the transmembrane domain is demonstrated
additional information
?
x * 64391, recombinant transmembrane domain-deleted enzyme mutant, mass spectrometry
additional information
three major cavities in the active site are the membrane access channel, the acyl-chain binding pocket, and the cytosolic port, overview. The core structure of the FAAH monomer adopts an alpha/beta fold with a twisted 11-strand beta-sheet in the center and 24 alpha-helices surrounding the sheet
additional information
three major cavities in the active site are the membrane access channel, the acyl-chain binding pocket, and the cytosolic port, overview. The core structure of the FAAH monomer adopts an alpha/beta fold with a twisted 11-strand beta-sheet in the center and 24 alpha-helices surrounding the sheet
