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
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Turnover Number on EC 3.5.1.99 - fatty acid amide hydrolase
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TURNOVER NUMBER [1/s] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.0022
oleamide
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pH 9.0, mutant enzyme S217A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification
0.055
oleamide
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pH 9.0, mutant enzyme S218A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification
3.3
oleamide
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pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain
4.4
oleamide
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pH 9.0, mutant enzyme H358A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification
5.2
oleamide
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pH 9.0, wild-type enzyme, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification
7.7
oleamide
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pH 9.0, mutant enzyme H449A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification
20
oleamide
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pH 9.0, mutant enzyme H184Q, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification
