Any feedback?
Information on EC 3.5.1.99 - fatty acid amide hydrolase and Organism(s) Rattus norvegicus and UniProt Accession P97612
for references in articles please use BRENDA:EC3.5.1.99Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.1.99 fatty acid amide hydrolaseIUBMB Comments
Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.
Specify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
=
+
Synonyms
fatty acid amide hydrolase, fatty-acid amide hydrolase, anandamide amidohydrolase, endocannabinoid-degrading enzyme, hfaah, oleamide hydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FAAH
-
FAAH
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oleamide + H2O = oleic acid + NH3
structure-function relationship and catalytic mechanism, overview
anandamide + H2O = arachidonic acid + ethanolamine
structure-function relationship and catalytic mechanism, overview
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
fatty acylamide amidohydrolase
Integral membrane protein, the enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide, occurs in mammalia.
CAS REGISTRY NUMBER
COMMENTARY
153301-19-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anandamide + H2O
ethanolamine + arachidonic acid
-
-
-
?
arachidonyl-7-amino-4-methylcoumarin amide + H2O
arachidonic acid + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide + H2O
4-(pyren-1-yl)butanamide + ethylene glycol
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
?
(11Z)-eicosenamide + H2O
(11Z)-eicosenoic acid + NH3
-
105% of the activity with oleamide
-
-
?
(12Z)-octadecenamide + H2O
(12Z)-octadecenoic acid + NH3
-
92% of the activity with oleamide
-
-
?
(13Z)-eicosenamide + H2O
(13Z)-eicosenoic acid + NH3
-
103% of the activity with oleamide
-
-
?
(13Z)-octadecenamide + H2O
(13Z)-octadecenoic acid + NH3
-
82% of the activity with oleamide
-
-
?
(15Z)-octadecenamide + H2O
(15Z)-octadecenoic acid + NH3
-
90% of the activity with oleamide
-
-
?
(5Z)-eicosenamide + H2O
(5Z)-eicosenoic acid + NH3
-
116% of the activity with oleamide
-
-
?
(5Z,8Z,11Z,14Z)-N-(2-fluoroethyl)icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolysis rate is 1.3fold higher than the rate of anandamide hydrolysis
-
-
?
(5Z,8Z,11Z,14Z)-N-(2-hydroxy-1,1-dimethylethyl)icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolyzed at 4.3% the rate of anandamide
-
-
?
(5Z,8Z,11Z,14Z)-N-(2-methylpropyl)icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolyzed at 2% the rate of anandamide
-
-
?
(5Z,8Z,11Z,14Z)-N-(3-hydroxyphenyl)icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolysis rate is 1.5fold higher than the rate of anandamide hydrolysis
-
-
?
(5Z,8Z,11Z,14Z)-N-(4-hydroxyphenyl)icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolyzed at 16% the rate of anandamide
-
-
?
(5Z,8Z,11Z,14Z)-N-tert-butylicosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolyzed at 1.8% the rate of anandamide
-
-
?
(5Z,8Z,11Z,14Z)-N-[(1S)-1-methylpropyl]icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolyzed at 6.3% the rate of anandamide
-
-
?
(5Z,8Z,11Z,14Z)-N-[(2R)-2-hydroxypropyl]icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolysis rate is 1.2fold higher than the rate of anandamide hydrolysis
-
-
?
(5Z,8Z,11Z,14Z)-N-[(2S)-2-hydroxypropyl]icosa-5,8,11,14-tetraenamide + H2O
?
-
hydrolyzed at 21% the rate of anandamide
-
-
?
(6Z)-octadecenamide + H2O
(6Z)-octadecenoic acid + NH3
-
91% of the activity with oleamide
-
-
?
(7Z)-octadecenamide + H2O
(7Z)-octadecenoic acid + NH3
-
109% of the activity with oleamide
-
-
?
(8Z)-eicosenamide + H2O
(8Z)-eicosenoic acid + NH3
-
112% of the activity with oleamide
-
-
?
(9E)-octadecenamide + H2O
(9E)-octadecenoic acid + NH3
-
52% of the activity with oleamide
-
-
?
(9Z)-N-(2-hydroxyethyl)octadec-9-enamide + H2O
?
-
hydrolyzed at 61% the rate of anandamide
-
-
?
(9Z)-tetradec-9-enamide + H2O
myristoleic acid + NH3
-
86% of the activity with oleamide
-
-
?
(9Z,12Z)-N-(2-hydroxyethyl)octadeca-9,12-dienamide + H2O
?
-
hydrolyzed at 75% the rate of anandamide
-
-
?
(9Z,12Z)-N-[(1R)-2-hydroxy-1-methylethyl]octadeca-9,12-dienamide + H2O
?
-
hydrolyzed at 20.5% the rate of anandamide
-
-
?
(9Z,12Z)-octadeca-9,12-dienamide + H2O
(9Z,12Z)-octadeca-9,12-dienoate + NH3
-
104% of the activity with oleamide
-
-
?
(R)-alpha-methanandamide + H2O
?
-
2.4% of the activity with anandamide
-
-
?
(R)-beta-methanandamide + H2O
?
-
121% of the activity with anandamide
-
-
?
(S)-alpha-methanandamide + H2O
?
-
23% of the activity with anandamide
-
-
?
(S)-beta-methanandamide + H2O
?
-
21% of the activity with anandamide
-
-
?
11,14,17-eicosatrienamide + H2O
11,14,17-eicosatrienoic acid + NH3
-
140% of the activity with oleamide
-
-
?
11,14-eicosadienamide + H2O
? + NH3
-
127% of the activity with oleamide
-
-
?
2,2-dimethyloleamide + H2O
2,2-dimethyloleic acid + NH3
-
3% of the activity with oleamide
-
-
?
2-methyloleamide + H2O
2-methyloleic acid + NH3
-
7% of the activity with oleamide
-
-
?
8,11,14-eicosatrienamide + H2O
8,11,14-eicosatrienoic acid + NH3
-
138% of the activity with oleamide
-
-
?
alpha-linolenamide + H2O
? + NH3
-
138% of the activity with oleamide
-
-
?
arachidonoyl 7-amido-4-methylcoumarin + H2O
arachidonic acid + 7-amino-4-methylcoumarin
-
-
-
-
?
beta-arachidonoylglycerol + H2O
?
-
hydrolysis is 2.5fold higher than the rate of anandamide hydrolysis
-
-
?
dodecanoamide + H2O
dodecanoic acid + NH3
-
74% of the activity with oleamide
-
-
?
linoelaidamide + H2O
(9E,12E)-octadeca-9,12-dienoic acid + NH3
-
54% of the activity with oleamide
-
-
?
N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide + H2O
4-pyren-1-ylbutanoic acid + ?
-
-
-
-
?
N-(2-hydroxyethyl)octadecanamide + H2O
?
-
hydrolyzed at 15.0% the rate of anandamide
-
-
?
N-(4-hydroxy-2-methylphenyl) arachidonoyl amide + H2O
4-amino-m-cresol + NH3
-
the rate of metabolism of VDM11 is about 1520% of that for anandamide
-
-
?
palmitoamide + H2O
palmitic acid + NH3
-
72% of the activity with oleamide
-
-
?
palmitoleamide + H2O
palmitoleic acid + NH3
-
79% of the activity with oleamide
-
-
?
stearamide + H2O
stearic acid + NH3
-
69% of the activity with oleamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
-
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
the enzyme is responsible for the hydrolysis of a number of neuromodulatory fatty acid amides, including the endogenous cannabinoid anandamide and the sleep-inducing lipid oleamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
the serine hydrolase is responsible for the degradation of endogenous oleamide and anandamide, fatty acid amides that function as chemical messengers
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
168% of the activity with oleamide
-
-
?
arachidonamide + H2O
arachidonic acid + NH3
-
311% of the activity with oleamide
-
-
?
myristic amide + H2O
myristic acid + NH3
-
24.3% of the activity with oleamide
-
-
?
myristic amide + H2O
myristic acid + NH3
-
24% of the activity with anandamide
-
-
?
myristic amide + H2O
myristic acid + NH3
-
83% of the activity with oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
-
-
-
?
oleamide + H2O
oleic acid + NH3
-
enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
role of FAAH in epithelial cells of the choroid plexus may be to control the concentration of oleamide in the cerebrospinal fluid. FAAH may exert an important regulatory role in shaping the duration and magnitude of the sleep-inducing effect of endogenously or exogenously derived oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
the enzyme is responsible for the hydrolysis of a number of neuromodulatory fatty acid amides, including the endogenous cannabinoid anandamide and the sleep-inducing lipid oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
the serine hydrolase is responsible for the degradation of endogenous oleamide and anandamide, fatty acid amides that function as chemical messengers
-
-
?
oleamide + H2O
oleic acid + NH3
-
serine residue 241 acts as the catalytic nucleophile of the enzyme. FAAH does not utilize a histidine base for the activation of its serine nucleophile
-
-
?
palmitic amide + H2O
palmitic acid + NH3
-
10% of the activity with anandamide
-
-
?
palmitic amide + H2O
palmitic acid + NH3
-
9.9% of the activity with oleamide
-
-
?
stearic amide + H2O
stearic acid + NH3
-
5.8% of the activity with anandamide
-
-
?
stearic amide + H2O
stearic acid + NH3
-
5.8% of the activity with oleamide
-
-
?
additional information
?
-
-
catalytic efficiency (kcat/Km) of FAAH for nonanoyl p-nitroanilide is approximately 50fold higher than for hexanoyl p-nitroanilide. NAI491 participates in hydrophobic binding interactions with medium-chain FAAH substrates. Use of p-nitroanilide substrates allows for the precise monitoring of enzymatic hydrolysis rates by following the increase in UV absorbance at 382 nm due to the release of p-nitroaniline. p-Nitroanilides are slower FAAH substrates than the corresponding primary amides, however, the binding affinities of these two classes of substrates are equivalent. Due to the slower rates of p-nitroanilide hydrolysis relative to the corresponding primary amides, it can be assumed that pNA substrates are hydrolyzed by FAAH in an acylation rate-limiting manner, allowing for the direct measurement of substrate binding constants through the determination of Km values
-
-
?
additional information
?
-
-
FAAH is an enzyme of broad substrate specificity and is capable of hydrolyzing a wide array of unsaturated, and to a lesser extent saturated, fatty acid primary amides. However, when substituted adjacent to the amide carbonyl, the substrates can be made sterically or electronically resistant to hydrolysis. Long chain saturated fatty acid amides are hydrolyzed slower than the corresponding Z unsaturated fatty acid amides and the rate of hydrolysis increases incrementally with increases in the degree of unsaturation
-
-
?
additional information
?
-
-
hybrid quantum mechanics/molecular mechanics (QM/MM) calculations reveal a new mechanism of nucleophile activation involving a LysSerSer catalytic triad. The proposed mechanism, shows that Lys142 and cis-Ser217 have a direct role in the activation of Ser241, in agreement with kinetic labelling experiments employing the highly reactive fluorophosphonatetetramethyl rhodamine. The greater reduction of Ser241 labelling rate in the K142A/S217A double mutant, compared to the K142A and S217A single mutants, suggests that Lys142 and Ser217 cooperate to deprotonate Ser241
-
-
?
additional information
?
-
-
N,N-bis(2-hydroxyethyl)arachidonamide is not hydrolyzed
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anandamide + H2O
ethanolamine + arachidonic acid
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
the enzyme is responsible for the hydrolysis of a number of neuromodulatory fatty acid amides, including the endogenous cannabinoid anandamide and the sleep-inducing lipid oleamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
the serine hydrolase is responsible for the degradation of endogenous oleamide and anandamide, fatty acid amides that function as chemical messengers
-
-
?
oleamide + H2O
oleic acid + NH3
-
enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
role of FAAH in epithelial cells of the choroid plexus may be to control the concentration of oleamide in the cerebrospinal fluid. FAAH may exert an important regulatory role in shaping the duration and magnitude of the sleep-inducing effect of endogenously or exogenously derived oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
the enzyme is responsible for the hydrolysis of a number of neuromodulatory fatty acid amides, including the endogenous cannabinoid anandamide and the sleep-inducing lipid oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
the serine hydrolase is responsible for the degradation of endogenous oleamide and anandamide, fatty acid amides that function as chemical messengers
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5-iodo-1,3-oxazol-2-yl)[(3R)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl]methanone
-
(5-iodo-1,3-oxazol-2-yl)[(3S)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl]methanone
-
1,1,1-trifluoro-N-([1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]carbamoyl)methanesulfonamide
-
1,3-oxazol-2-yl[(2R)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl]methanone
-
1,3-oxazol-2-yl[(2S)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl]methanone
-
1,3-oxazol-2-yl[(3R)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl]methanone
-
1,3-oxazol-2-yl[(3R)-7-phenyl-3,4-dihydro-2H-chromen-3-yl]methanone
-
1,3-oxazol-2-yl[(3S)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl]methanone
-
1,3-oxazol-2-yl[(3S)-7-phenyl-3,4-dihydro-2H-chromen-3-yl]methanone
-
1-(4-benzylpiperazin-1-yl)-2-[4-(2-methylpropyl)phenyl]propan-1-one
18% inhibition at 0.1 mM
1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one
the compound belongs to the ketobenzimidazoles, though containing a carbonyl moiety, that do not covalently modify Ser241. These inhibitors achieve potent inhibition of FAAH activity primarily from shape complementarity to the active site and through numerous hydrophobic interactions exhibiting excellent selectivity and good pharmacokinetic properties, nonmechanism-based inhibition. Pharmacokinetic parameters and selectivity 2, overview
1-[4-(2,3-dimethylphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-(2-methylphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
33% inhibition at 0.1 mM
1-[4-(3,4-dichlorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-(3-chlorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-(3-methoxyphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
41% inhibition at 0.1 mM
1-[4-(3-methylphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-(4-chlorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-(4-fluorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-(4-methoxyphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
-
1-[4-[(3-chlorophenyl)methyl]piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
8% inhibition at 0.1 mM
2-(2-fluorobiphenyl-4-yl)-N-(2-(3-methylpyridin-2-ylamino)-2-oxoethyl)propanamide
-
2-(2-fluorobiphenyl-4-yl)-N-(3-methylpyridin-2-yl)propanamide
mode of inhibition, overview. Flu-AM1 does not inhibit the enzyme from brain in vivo
2-(4-cyclohexylphenoxy)-N-[2-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-(4-cyclohexylphenoxy)-N-[3-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-(4-cyclohexylphenoxy)-N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-(4-cyclohexylphenoxy)-N-[4-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-(4-cyclohexylphenoxy)-N-[4-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-(methylamino)-2-oxoethyl [2-[1-(6-methylpyridin-2-yl)piperidin-4-yl]ethyl]carbamate
-
2-methyl-N-(3-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[2-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[3-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[4-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[4-(2-methylpropyl)phenyl]-1-(4-phenylpiperazin-1-yl)propan-1-one
-
2-[4-(2-methylpropyl)phenyl]-N-[[3-(trifluoromethyl)phenyl]methyl]propanamide
-
2-[4-(2-methylpropyl)phenyl]-N-[[4-(trifluoromethyl)phenyl]methyl]propanamide
-
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[2-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[3-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[4-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
-
4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[2-(2,4-difluorophenyl)pyridin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[2-(2,4-difluorophenyl)pyrimidin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[3-(4-chlorophenoxy)benzyl]-N-(pyridin-3-yl)piperazine-1-carboxamide
-
4-[4-(2,3-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[4-(2,4-difluorophenyl)-1,3-thiazol-2-yl]-N-(3,4-dimethyl-1,2-oxazol-5-yl)piperazine-1-carboxamide
-
4-[4-(2,4-difluorophenyl)pyridin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[4-(2,4-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[4-(2,5-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[4-(3,4-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[4-(3,5-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[6-(2,4-difluorophenyl)pyridin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
4-[6-(2,4-difluorophenyl)pyrimidin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide
an irreversible covalent inhibitor, binding structure, overview
hexadecyl sulfonylfluoride
i.e. AM374, is a potent in vitro and in vivo inhibitor of fatty acid amide hydrolase
methyl 6-(2-[[(2R)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl]carbonyl]-1,3-oxazol-5-yl)pyridine-2-carboxylate
-
methyl 6-(2-[[(2S)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl]carbonyl]-1,3-oxazol-5-yl)pyridine-2-carboxylate
-
methyl 6-(2-[[(3R)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl]carbonyl]-1,3-oxazol-5-yl)pyridine-2-carboxylate
-
methyl 6-(2-[[(3S)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl]carbonyl]-1,3-oxazol-5-yl)pyridine-2-carboxylate
-
N-(1,4-dihydroquinolin-8-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(2-methylphenyl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(3,4-dimethyl-1,2-oxazol-5-yl)-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
-
N-(3-bromopyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(3-chloropyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(3-iodopyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclobutane-1-carboxamide
-
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclohexane-1-carboxamide
30% inhibition at 0.1 mM
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclopentane-1-carboxamide
-
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclopropane-1-carboxamide
-
N-(3-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)acetamide
-
N-(3-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(3-methylpyridin-2-yl)-2-(4-[[7-(trifluoromethyl)quinolin-4-yl]amino]phenyl)propanamide
-
N-(3-methylpyridin-2-yl)-2-(4-[[8-(trifluoromethyl)quinolin-4-yl]amino]phenyl)propanamide
-
N-(4-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(5-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(pyrazin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(pyridazin-3-yl)-4-(3-[[5-(trifluoromethyl)pyridin-2-yl]oxy]benzylidene)piperidine-1-carboxamide
-
N-(pyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(pyridin-3-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(pyridin-4-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-(pyrimidin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-([1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]carbamoyl)benzenesulfonamide
-
N-([1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]carbamoyl)methanesulfonamide
-
N-phenyl-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
-
N-[(2,4-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(2,5-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(2,6-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
19% inhibition at 0.1 mM
N-[(2-chlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(2-methoxyphenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(3,4-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(3-hydroxy-4-methoxyphenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(4-methoxyphenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
-
N-[(pyridin-2-yl)methyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-[(pyridin-3-yl)methyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-[1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]-N'-phenylurea
-
N-[2-[(3-methylpyridin-2-yl)amino]-2-oxoethyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-[3-(trifluoromethyl)pyridin-2-yl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]-2-[4-(propan-2-yl)phenoxy]acetamide
-
N-[4-(2,3-dimethylphenyl)piperazin-1-yl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
24% inhibition at 0.1 mM
N-[4-(2-methylphenyl)piperazin-1-yl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
24% inhibition at 0.1 mM
N-[4-(4-chlorophenyl)piperazin-1-yl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
-
PF-3845
crystal structure analysis of enzyme-inhibitor complex. The inhibitor interacts with the catalytic triad and oxyanion hole residues
phenyl ([4-[(5-phenyl-2H-tetrazol-2-yl)methyl]phenyl]methyl)carbamate
-
phenyl 4-[2-(4-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
phenyl 4-[2-(5-chloro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
phenyl 4-[2-(5-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
phenyl 4-[2-(5-methoxy-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
phenyl 4-[2-(5-methyl-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
phenyl 4-[2-(6-fluoro-1H-indol-1-yl)ethyl]piperazine-1-carboxylate
-
phenyl 4-[2-(6-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
phenyl 4-[2-(7-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
-
[(2R)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(2S)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(3R)-7-(benzyloxy)-3,4-dihydro-2H-chromen-3-yl](1,3-oxazol-2-yl)methanone
-
[(3R)-7-(benzyloxy)-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(3R)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(3R)-7-phenyl-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(3S)-7-(benzyloxy)-3,4-dihydro-2H-chromen-3-yl](1,3-oxazol-2-yl)methanone
-
[(3S)-7-(benzyloxy)-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(3S)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[(3S)-7-phenyl-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
-
[1-[(2,6-difluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(2-chlorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(2-fluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(4-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
[1-[(3,5-difluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(3,5-dimethoxyphenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(3-chlorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(3-fluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(4-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
(1-benzylpiperidin-4-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
(4-benzylpiperazin-1-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
(5E)-5-(4-methoxybenzylidene)-3-[1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indol-5-yl]-1,3-thiazolidine-2,4-dione
-
-
(5Z,8Z,11Z,14Z)-N-((2,2-dimethyl-1,3-dioxolan-4-yl)methyl)icosa-5,8,11,14-tetraenamide
-
-
(5Z,8Z,11Z,14Z)-N-[(2R)-tetrahydrofuran-2-ylmethyl]icosa-5,8,11,14-tetraenamide
-
-
(5Z,8Z,11Z,14Z)-N-[(2S)-tetrahydrofuran-2-ylmethyl]icosa-5,8,11,14-tetraenamide
-
-
(6aR,10aR)-3-(1,1-dimethylheptyl)-9-(hydroxymethyl)-6,6-dimethyl-6a,7,10,10a-tetrahydro-6H-benzo[c]chromen-1-ol
-
-
1-(2-oxo-3-[4-[4-(trifluoromethyl)phenoxy]phenoxy]propyl)-1H-indole-5-carboxylic acid
-
21% inhibition at 0.01 mM
1-(2-oxo-3-[[4'-(propan-2-yl)biphenyl-4-yl]oxy]propyl)-1H-indole-5-carboxylic acid
-
-
1-[1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indol-5-yl]-1H-benzimidazole-7-carboxylic acid
-
-
1-[2-oxo-3-[4-(2-phenoxyethoxy)phenoxy]propyl]-1H-indole-5-carboxylic acid
-
-
1-[2-oxo-3-[4-(2-phenylpropan-2-yl)phenoxy]propyl]-1H-indole-5-carboxylic acid
-
-
1-[3-(4-octylphenoxy)-2-oxopropyl]indole-5-carboxylic acid
-
structure-activity relationship, overview
1-[3-[(3'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(3'-fluorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(3-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(3-fluorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(3-methoxybiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(3-methylbiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
39% inhibition at 0.01 mM
1-[3-[(4'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(4'-fluorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(4'-methoxybiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[(4'-methylbiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
1-[3-[4-(4-fluorophenyl)phenoxy]-2-oxopropyl]indazole-5-carboxylic acid
-
-
1-[5-(2,4-dimethoxypyrimidin-5-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
1-[5-(2,6-dimethoxypyrimidin-4-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
1-[5-(3-benzyl-1,2,4-oxadiazol-5-yl)-1H-indol-1-yl]-3-(4-octylphenoxy)propan-2-one
-
-
1-[5-(3-ethyl-1,2,4-oxadiazol-5-yl)-1H-indol-1-yl]-3-(4-octylphenoxy)propan-2-one
-
-
1-[5-(morpholin-4-ylcarbonyl)-1H-indol-1-yl]-3-(4-octylphenoxy)propan-2-one
-
-
1-[5-[(4-methylpiperazin-1-yl)carbonyl]-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
2,2-dimethyl-1,3-dioxolan-4-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
2-(5,5-dimethyl-1,3-dioxan-2-yl)ethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N,N-diethylazetidine-1-carboxamide
-
-
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-ethyl-N-(2-hydroxyethyl)azetidine-1-carboxamide
-
-
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methyl-N-(2-phenylethyl)azetidine-1-carboxamide
-
-
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methyl-N-phenylazetidine-1-carboxamide
-
-
4-(3-phenyl-[1,2,4]thiadiazol-5-yl)piperazine-1-carboxylic acid phenylamide
-
JNJ-1661010
4-(acetylamino)phenyl (4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)acetate
-
-
4-(acetylamino)phenyl 2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoate
-
competitive, also able to inhibit the FAAH activity in rat basophilic leukemia cells as assessed by measuring either the hydrolysis of anandamide, the FAAH-dependent cellular accumulation of anandamide, or the FAAH-dependent recycling of tritium to the cellmembranes
4-(acetylamino)phenyl 2-[[2-(trifluoromethyl)pyridin-4-yl]amino]pyridine-3-carboxylate
-
-
4-(acetylamino)phenyl 2-[[3-(trifluoromethyl)phenyl]amino]pyridine-3-carboxylate
-
-
4-(acetylamino)phenyl 2-{[2-(trifluoromethyl)pyridin-4-yl]amino}benzoate
-
-
4-(acetylamino)phenyl 3-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoate
-
-
4-(acetylamino)phenyl 3-methyl-4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
-
-
4-(acetylamino)phenyl 3-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
-
-
4-(acetylamino)phenyl 4-([[2-(trifluoromethyl)pyridin-4-yl]amino]methyl)benzoate
-
-
4-(acetylamino)phenyl 4-chloro-2-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
-
-
4-(acetylamino)phenyl 4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
-
-
4-(acetylamino)phenyl 5-chloro-2-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
-
-
4-(acetylamino)phenyl 5-methyl-2-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
-
-
4-(acetylamino)phenyl N-(3-methyl-4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoyl)glycinate
-
-
4-(acetylamino)phenyl N-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoyl)glycinate
-
-
4-(acetylamino)phenyl N-[(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)acetyl]glycinate
-
-
4-(acetylamino)phenyl N-[2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoyl]glycinate
-
-
5-(4-chlorophenyl)-1-(2,4-dichlorophenyl)-4-methyl-N-morpholin-4-yl-1H-pyrazole-3-carboxamide
-
-
7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one
-
OL-135, an alpha-keto-heterocycle that is a covalent reversible inhibitor of FAAH
7-phenyl-1-[5-(thiomorpholin-4-ylcarbonyl)-1,3-oxazol-2-yl]heptan-1-one
-
-
7-phenyl-1-[5-[4-(trifluoromethyl)pyridin-2-yl]-1,3-oxazol-2-yl]heptan-1-one
-
-
azepan-1-yl[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
azetidin-1-yl[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
ethoxy oleoyl fluorophosphonate
-
irreversible inhibitor, exclusively modifies FAAH at S241
methyl 5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]thiophene-2-carboxylate
-
-
N,N-dibenzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
-
-
N,N-dimethyl-1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-carboxamide
-
-
N,N-dimethyl-1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-sulfonamide
-
-
N-(4-hydroxy-2-methylphenyl) arachidonoyl amide
-
i.e. VDM11, inhibits the metabolism of anandamide by rat brain FAAH. Inhibition may at least in part be a consequence of the compound acting as an alternative substrate
N-(4-hydroxyphenyl)-5Z,8Z,11Z,14Z-eicosatetraenamide
-
i.e. AM404, a bioactive N-acylphenolamine, derived from paracetamol, competitve inhibition
N-(4-hydroxyphenyl)arachidonylamide
-
i.e. AM404, inhibits the metabolism of anandamide by rat brain FAAH
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-(2-hydroxyethyl)azetidine-1-carboxamide
-
-
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methylazetidine-1-carboxamide
-
-
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-[2-(dimethylamino)ethyl]azetidine-1-carboxamide
-
-
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
-
-
N-benzyl-3-[(R)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methylazetidine-1-carboxamide
-
-
N-benzyl-3-[(S)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methylazetidine-1-carboxamide
-
-
N-tert-butyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
-
-
N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide
-
a reversible, albeit slowly dissociating inhibitor of FAAH, reversibly and noncovalently inhibiting, molecular docking and computational modeling of interactions of the benzothiazole analogue 1 with humanized rat FAAH by induced fit docking, overview. Failure to observe the formation of covalent enzyme-inhibitor adduct or putative cleavage product using electrospray mass spectrometric techniques
tetrahydro-2H-pyran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
[3-[(2-chlorophenyl)(4-chlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(2-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(2-chloropyridin-3-yl)(3,4-dichlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(2-chloropyridin-3-yl)(3-methoxyphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(2-chloropyridin-3-yl)(phenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(3-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-hydroxypiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-methylpiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3,4-dihydroisoquinolin-2(1H)-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypyrrolidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-methylpiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4,4-difluoropiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-fluoropiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-hydroxypiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperazin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](morpholin-4-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](pyrrolidin-1-yl)methanone
-
-
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
-
-
[3-[(4-chlorophenyl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(6-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(S)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[1,3-benzodioxol-5-yl(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[phenyl(pyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
3'-carbamoylbiphenyl-3-yl cyclohexylcarbamate
covalent enzyme binding at Ser241 leading to irreversible inhibition, the attack at the carbonyl group by Ser 241 leads to the formation of carbamoylated, catalytically inactive FAAH and releasing the O-biphenyl moiety as the leaving group
5-(4-hydroxyphenyl)pentanesulfonyl fluoride
i.e. AM3506, irreversible inhibitor for both the rat and the human enzyme
7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one
i.e. OL-135, the enzyme inhibitor exhibits antinociceptive and anti-inflammatory activity and increases levels of anandamide in vivo
URB597
a carbamate inhibitor that displays excellent selectivity for FAAH in the nervous system, although the inhibitor does inactivate additional peripheral hydrolases, enzyme-inhibitor binding structure, overview. The inhibitor interacts with the catalytic triad and oxyanion hole residues
URB597
-
a carbamate inhibiting FAAH covalently and irreversibly, time-dependent inhibition, overview
additional information
design and synthesis of 2-oxoheterocycle inhibitors of fatty acid amide hydrolase, a 6-phenoxychroman-2-yl-2-ketooxazole series, and a 7-arylchroman-3-yl-2-ketooxazole series. Evaluation and role of conformational constraintsin the acyl side chain, overview
-
additional information
design, synthesis, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase inhibitors, overview
-
additional information
O-(triazolyl)methyl carbamates as potent fatty acid amide hydrolase inhibitors, overview. These compounds show improved stability in rat plasma and kinetic solubility in buffer with respect to the lead compound O-(1,2,3-triazol-4-yl)methyl carbamate
-
additional information
sulfonyl fluoride inhibitors of fatty acid amide hydrolase, structure-activity relationship, docking and molecular modeling, overview
-
additional information
FAAH inhibition represents a promising strategy to activate the cannabinoid system, since it does not result in the psychotropic and peripheral side effects characterizing the agonists of the cannabinoid receptors
-
additional information
structure-activity relationship studies on a series of aryl N-(omega-imidazolyl- and omega-tetrazolylalkyl)carbamate inhibitors are investigated. A pronounced increase in inhibitory potency is observed if a phenyl residue attached to the carbamate oxygen atom is replaced by a pyridin-3-yl moiety. The most active compounds exhibit IC50 values in the low nanomolar range. Investigations on the metabolic properties of these inhibitors are performed. In rat liver homogenate and in porcine plasma, the extent of their degradation is shown to be strongly dependent on the kind of aryl residue bound to the carbamate as well as on the length and type of the alkyl spacer connecting the carbamate group with the heterocyclic system
-
additional information
-
a series of 5-substituted 7-phenyl-1-(oxazol-2-yl)heptan-1-ones are prepared and evaluated for FAAH inhibitory potency as well as FAAH selectivity versus competitive serine proteases
-
additional information
-
paracetamol itself does not inhibit FAAH, but undergoes a FAAH-dependent two-step metabolic transformation in the brain, liver, and spinal cord to form the bioactive N-acylphenolamine AM404. Synthesis and evaluation of paracetamol ester enzyme inhibitors, structure-activity relationship studies, overview
-
additional information
-
1-(3-biaryloxy-2-oxopropyl)indole-5-carboxylic acids and related compounds can act as dual inhibitors of cytosolic phospholipase A2alpha, EC 3.1.1.4, and fatty acid amide hydrolase, overview. Substituents at the indole 3- and 5-positions and replacement of the indole scaffold of this compound by other heterocycles strongly influences the inhibitory potency against FAAH. No inhibition by 1-[3-(biphenyl-2-yloxy)-2-oxopropyl]-1H-indole-5-carboxylic acid, N-methyl-1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-carboxamide, N,N-dimethyl-1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-carboxamide, 1-[5-(morpholin-4-ylcarbonyl)-1H-indol-1-yl]-3-(4-octylphenoxy)propan-2-one, (5E)-5-(4-methoxybenzylidene)-3-[1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indol-5-yl]-1,3-thiazolidine-2,4-dione, 1-[5-(3-benzyl-1,2,4-oxadiazol-5-yl)-1H-indol-1-yl]-3-(4-octylphenoxy)propan-2-one, 1-[5-(3-ethyl-1,2,4-oxadiazol-5-yl)-1H-indol-1-yl]-3-(4-octylphenoxy)propan-2-one, 1-[1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indol-5-yl]-1H-benzimidazole-7-carboxylic acid, and 1-(4-octylphenoxy)-3-[5-(1H-tetrazol-5-yl)-1H-indol-1-yl]propan-2-one at 0.01 mM
-
additional information
-
mechanism of inhibition of fatty acid amide hydrolase by sulfonamide-containing benzothiazoles, long residence time derived from increased kinetic barrier and not exclusively from thermodynamic potency, transition-state analogues, overview
-
additional information
-
tetra-substituted azetidine ureas with in vivo activity as fatty acid amide hydrolase inhibitors, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
oleamide
-
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
0.011
oleamide
-
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
0.012
oleamide
-
pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain
0.015
oleamide
-
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
0.015
oleamide
-
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
0.029
oleamide
-
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
0.03
oleamide
-
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0022
oleamide
-
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
-
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
-
pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain
4.4
oleamide
-
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
-
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
-
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
-
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000047
7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one
pH 9.0, 22°C
0.000026
1-[5-(2,4-dimethoxypyrimidin-5-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.000005
1-[5-(2,6-dimethoxypyrimidin-4-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.000015
1-[5-(3-methylpyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.000025
1-[5-(4-aminopyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.000002
1-[5-(4-fluoropyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.0000008
1-[5-(4-methoxypyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.0000006
1-[5-(4-methylpyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.0000032
1-[5-(4-nitropyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.0000028
1-[5-(5-methylpyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.0000033
1-[5-(6-methylpyridin-2-yl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.000024
1-[5-(morpholin-4-ylcarbonyl)-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.00008
1-[5-[(4-methylpiperazin-1-yl)carbonyl]-1,3-oxazol-2-yl]-7-phenylheptan-1-one
-
-
0.0000011
2-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-4-carbonitrile
-
-
0.00005
2-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-4-carboxylic acid
-
-
0.00016
4-(acetylamino)phenyl 2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoate
-
pH 7.4, 37°C
0.000015
5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]furan-2-carboxylic acid
-
-
0.00035
5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyrimidine-2,4(1H,3H)-dione
-
-
0.000011
5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]thiophene-2-carboxylic acid
-
-
0.000003
5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]thiophene-2-sulfonamide
-
-
0.000001
6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxamide
-
-
0.00002
6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid
-
-
0.0000012
6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-3-carboxamide
-
-
0.000007
6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-3-carboxylic acid
-
-
0.000012
6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyrimidine-2,4(1H,3H)-dione
-
-
0.000008
7-phenyl-1-[5-(piperidin-1-ylcarbonyl)-1,3-oxazol-2-yl]heptan-1-one
-
-
0.00001
7-phenyl-1-[5-(thiomorpholin-4-ylcarbonyl)-1,3-oxazol-2-yl]heptan-1-one
-
-
0.005
7-phenyl-1-[5-[2-(trifluoroacetyl)phenyl]-1,3-oxazol-2-yl]heptan-1-one
-
-
0.000016
7-phenyl-1-[5-[3-(trifluoroacetyl)phenyl]-1,3-oxazol-2-yl]heptan-1-one
-
-
0.000065
7-phenyl-1-[5-[4-(trifluoroacetyl)phenyl]-1,3-oxazol-2-yl]heptan-1-one
-
-
0.0000035
7-phenyl-1-[5-[4-(trifluoromethyl)pyridin-2-yl]-1,3-oxazol-2-yl]heptan-1-one
-
-
0.00013
methyl 2-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-3-carboxylate
-
-
0.0000013
methyl 2-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-4-carboxylate
-
-
0.0000055
methyl 5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]furan-2-carboxylate
-
-
0.000007
methyl 5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]thiophene-2-carboxylate
-
-
0.000008
methyl 6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylate
-
-
0.0000035
methyl 6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-3-carboxylate
-
-
0.0026
N-(4-hydroxy-2-methylphenyl) arachidonoyl amide
-
in the presence of fatty acid-free bovine serum albumin (0.125% w/v). In the absence of fatty acid-free bovine serum albumin, the IC50 value is reduced
0.0021
N-(4-hydroxyphenyl)arachidonylamide
-
in the presence of fatty acid-free bovine serum albumin (0.125% w/v). In the absence of fatty acid-free bovine serum albumin, the IC50 value is reduced
additional information
additional information
-
time-dependent inhibition kinetics with N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide, recombinant enzyme not purified, detailed overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
1,1,1-trifluoro-N-([1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]carbamoyl)methanesulfonamide
Rattus norvegicus
37°C, pH 7.4
0.000024
1-(1H-benzotriazol-1-yl)-3-(4-phenoxyphenoxy)propan-2-one
Rattus norvegicus
pH and temperature not specified in the publication
0.0016
1-(1H-benzotriazol-1-yl)-3-[(4-phenoxyphenyl)thio]propan-2-one
Rattus norvegicus
pH and temperature not specified in the publication
0.0001
1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one
Rattus norvegicus
pH and temperature not specified in the publication
0.0017
1-[4-(2,3-dimethylphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.016
1-[4-(3,4-dichlorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.0017
1-[4-(3-chlorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.016
1-[4-(3-methylphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.0017
1-[4-(4-chlorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.017
1-[4-(4-fluorophenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.0045
1-[4-(4-methoxyphenyl)piperazin-1-yl]-2-[4-(2-methylpropyl)phenyl]propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.017
2-(2-fluorobiphenyl-4-yl)-N-(2-(3-methylpyridin-2-ylamino)-2-oxoethyl)propanamide
Rattus norvegicus
pH 7.4, 37°C
0.00044
2-(2-fluorobiphenyl-4-yl)-N-(3-methylpyridin-2-yl)propanamide
Rattus norvegicus
pH 7.4, 37°C
0.00065
2-(4-cyclohexylphenoxy)-N-[2-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.047
2-(4-cyclohexylphenoxy)-N-[3-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.0026
2-(4-cyclohexylphenoxy)-N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.0015
2-(4-cyclohexylphenoxy)-N-[4-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.00035
2-(4-cyclohexylphenoxy)-N-[4-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.00074
2-(6-methoxynaphthalen-2-yl)-N-(3-methylpyridin-2-yl)propanamide
Rattus norvegicus
pH 7.4, 37°C
0.00033
2-fluorophenyl [6-(5-phenyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.0018
2-methyl-N-(3-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.0011
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[2-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.013
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[3-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.00063
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.00062
2-[([1,1'-biphenyl]-4-yl)oxy]-N-[4-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.0047
2-[4-(2-methylpropyl)phenyl]-1-(4-phenylpiperazin-1-yl)propan-1-one
Rattus norvegicus
37°C, pH 7.4
0.0052
2-[4-(2-methylpropyl)phenyl]-N-(3-methylpyridin-2-yl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.028
2-[4-(2-methylpropyl)phenyl]-N-[[3-(trifluoromethyl)phenyl]methyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.051
2-[4-(2-methylpropyl)phenyl]-N-[[4-(trifluoromethyl)phenyl]methyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.0055
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[2-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.073
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[3-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.017
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.064
2-[[(2E)-hex-2-en-1-yl]oxy]-N-[4-(1H-imidazo[4,5-b]pyridin-2-yl)phenyl]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.00000442
3-pyridyl 4-(phenylcarbamoyl)piperidine-1-carboxylate
Rattus norvegicus
pH 8.0, 37°C, wild-type enzyme
0.0000033
4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.0000012
4-(4-benzyloxyphenoxy)butanesulfonyl fluoride
Rattus norvegicus
pH 7.4, 25°C
0.00066
4-fluorophenyl [6-(5-phenyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000012
4-[2-(2,4-difluorophenyl)pyridin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.000034
4-[2-(2,4-difluorophenyl)pyrimidin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.0000012
4-[4-(2,3-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.00000046
4-[4-(2,4-difluorophenyl)-1,3-thiazol-2-yl]-N-(3,4-dimethyl-1,2-oxazol-5-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.0000043 - 0.000074
4-[4-(2,4-difluorophenyl)pyridin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
0.00000043
4-[4-(2,4-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.00000017
4-[4-(2,5-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.00000028
4-[4-(3,4-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.00000034
4-[4-(3,5-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.000013
4-[6-(2,4-difluorophenyl)pyridin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.0000017
4-[6-(2,4-difluorophenyl)pyrimidin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.0000015
5-(4-benzyloxyphenyl)pentanesulfonyl fluoride
Rattus norvegicus
pH 7.4, 25°C
0.000036
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide
Rattus norvegicus
pH and temperature not specified in the publication
0.0000043
7-(2-benzyloxyphenyl)heptanesulfonyl fluoride
Rattus norvegicus
pH 7.4, 25°C
0.0000036
7-(3-benzyloxyphenyl)heptanesulfonyl fluoride
Rattus norvegicus
pH 7.4, 25°C
0.000269
7-(4-benzyloxyphenyl)heptane-1-sulfonic acid methyl ester
Rattus norvegicus
pH 7.4, 25°C
0.0000037
7-(4-benzyloxyphenyl)heptanesulfonyl fluoride
Rattus norvegicus
pH 7.4, 25°C
0.0043
N-(1,4-dihydroquinolin-8-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.00074
N-(2-methylphenyl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.0000013
N-(3,4-dimethyl-1,2-oxazol-5-yl)-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.00013
N-(3-bromopyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.000058
N-(3-chloropyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.00013
N-(3-iodopyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.0091
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclobutane-1-carboxamide
Rattus norvegicus
37°C, pH 7.4
0.06
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclopentane-1-carboxamide
Rattus norvegicus
37°C, pH 7.4
0.014
N-(3-methylpyridin-2-yl)-1-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)cyclopropane-1-carboxamide
Rattus norvegicus
37°C, pH 7.4
0.048
N-(3-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)acetamide
Rattus norvegicus
37°C, pH 7.4
0.00059
N-(3-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.0031
N-(3-methylpyridin-2-yl)-2-(4-[[7-(trifluoromethyl)quinolin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.027
N-(3-methylpyridin-2-yl)-2-(4-[[8-(trifluoromethyl)quinolin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.004
N-(4-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.011
N-(5-methylpyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.002
N-(pyrazin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.012
N-(pyridin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.0064
N-(pyridin-3-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.052
N-(pyridin-4-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.00099
N-(pyrimidin-2-yl)-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.027
N-([1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]carbamoyl)benzenesulfonamide
Rattus norvegicus
37°C, pH 7.4
0.027
N-([1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]carbamoyl)methanesulfonamide
Rattus norvegicus
37°C, pH 7.4
0.0000012
N-phenyl-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.021
N-[(2,4-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.0044
N-[(2,5-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.0041
N-[(2-chlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.018
N-[(2-methoxyphenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.036
N-[(3,4-dichlorophenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.018
N-[(3-hydroxy-4-methoxyphenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.043
N-[(4-methoxyphenyl)methyl]-2-[4-(2-methylpropyl)phenyl]propanamide
Rattus norvegicus
37°C, pH 7.4
0.023
N-[(pyridin-2-yl)methyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.032
N-[(pyridin-3-yl)methyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.021
N-[1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indazol-5-yl]-N'-phenylurea
Rattus norvegicus
37°C, pH 7.4
0.0024 - 0.027
N-[2-[(3-methylpyridin-2-yl)amino]-2-oxoethyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
0.00033
N-[3-(trifluoromethyl)pyridin-2-yl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.018
N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]-2-phenoxyacetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.0021
N-[3-([1,3]oxazolo[4,5-b]pyridin-2-yl)phenyl]-2-[4-(propan-2-yl)phenoxy]acetamide
Rattus norvegicus
assay in brain homogenates, substrate ananamide, pH and temperature not specified in the publication
0.017
N-[4-(4-chlorophenyl)piperazin-1-yl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.00026
phenyl ([4-[(5-phenyl-2H-tetrazol-2-yl)methyl]phenyl]methyl)carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00987
phenyl 4-[(1H-indol-1-yl)methyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00011
phenyl 4-[2-(1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00011
phenyl 4-[2-(4-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00041
phenyl 4-[2-(5-chloro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00097
phenyl 4-[2-(5-cyano-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00013
phenyl 4-[2-(5-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00036
phenyl 4-[2-(5-methoxy-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00074
phenyl 4-[2-(5-methyl-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00081
phenyl 4-[2-(6-fluoro-1H-indol-1-yl)ethyl]piperazine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.000046
phenyl 4-[2-(6-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.000052
phenyl 4-[2-(7-fluoro-1H-indol-1-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00041
phenyl 4-[2-(9H-carbazol-9-yl)ethyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00057
phenyl 4-[3-(1H-indol-1-yl)propyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00018
phenyl 4-[4-(1H-indol-1-yl)butyl]piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.0052
phenyl [2-[2-(5-phenyl-2H-tetrazol-2-yl)ethoxy]ethyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00096
phenyl [4-(1H-indol-1-yl)butyl]carbamate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.000094
phenyl [5-(1H-indol-1-yl)pentyl]carbamate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00043
phenyl [5-(2-phenyl-1H-imidazol-1-yl)pentyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00049
phenyl [5-(5-phenyl-2H-tetrazol-2-yl)pentyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.006
phenyl [6-(1H-imidazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00025
phenyl [6-(1H-indol-1-yl)hexyl]carbamate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00047
phenyl [6-(2-methyl-4,5-diphenyl-1H-imidazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00029
phenyl [6-(2-phenyl-1H-imidazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00049
phenyl [6-(4,5-diphenyl-1H-imidazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00088
phenyl [6-(4-phenyl-1H-imidazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00025
phenyl [6-(5-benzyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00048
phenyl [6-(5-phenyl-1H-imidazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.0013
phenyl [6-(5-phenyl-1H-tetrazol-1-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00062
phenyl [6-(5-phenyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000054
phenyl [6-[2-(3-chlorophenyl)-1H-imidazol-1-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000112
phenyl [6-[2-(3-fluorophenyl)-1H-imidazol-1-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00029
phenyl [6-[2-(3-methoxyphenyl)-1H-imidazol-1-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000075
phenyl [6-[2-(3-methylphenyl)-1H-imidazol-1-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00042
phenyl [6-[2-(4-chlorophenyl)-1H-imidazol-1-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000209
phenyl [6-[5-(2-chlorophenyl)-2H-tetrazol-2-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00018
phenyl [6-[5-(3-chlorophenyl)-2H-tetrazol-2-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00057
phenyl [6-[5-(4-chlorophenyl)-2H-tetrazol-2-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00028
phenyl [6-[5-(pyridin-2-yl)-2H-tetrazol-2-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00074
phenyl [6-[5-(pyridin-3-yl)-2H-tetrazol-2-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.0012
phenyl [6-[5-(pyridin-4-yl)-2H-tetrazol-2-yl]hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000093
phenyl [7-(1H-indol-1-yl)heptyl]carbamate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.00024
phenyl [7-(2-phenyl-1H-imidazol-1-yl)heptyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000081
phenyl [7-(5-phenyl-2H-tetrazol-2-yl)heptyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00024
phenyl [8-(1H-indol-1-yl)octyl]carbamate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.0004
phenyl [8-(2-phenyl-1H-imidazol-1-yl)octyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.000112
phenyl [8-(5-phenyl-2H-tetrazol-2-yl)octyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00000442
pyridin-3-yl 4-(phenylcarbamoyl)piperidine-1-carboxylate
Rattus norvegicus
37°C, pH 8.0
0.000011
pyridin-3-yl [6-(5-phenyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00007
[(2R)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
Rattus norvegicus
pH 9.0, 22°C
0.00005
[(2S)-6-phenoxy-3,4-dihydro-2H-chromen-2-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
Rattus norvegicus
pH 9.0, 22°C
0.00009
[(3R)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
Rattus norvegicus
pH 9.0, 22°C
0.00046
[(3S)-7-phenoxy-3,4-dihydro-2H-chromen-3-yl][5-(pyridin-2-yl)-1,3-oxazol-2-yl]methanone
Rattus norvegicus
pH 9.0, 22°C
0.0000119
[1-[(2,6-difluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000062
[1-[(2-chlorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000099
[1-[(2-fluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000014
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000032
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000076
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(4-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000104
[1-[(3,5-difluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000105
[1-[(3,5-dimethoxyphenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000132
[1-[(3-chlorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000121
[1-[(3-fluorophenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000118
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000098
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000039
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
Rattus norvegicus
pH 7.4, 37°C
0.0000058
[1-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(4-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
Rattus norvegicus
pH 7.4, 37°C
0.000237
(1-benzylpiperidin-4-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.006
(2R)-oxiran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.012
(2S)-oxiran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.00037
(4-benzylpiperazin-1-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.09
(5Z,8Z,11Z,14Z)-N-((2,2-dimethyl-1,3-dioxolan-4-yl)methyl)icosa-5,8,11,14-tetraenamide
Rattus norvegicus
-
37°C, substrate: anandamide
0.069
(5Z,8Z,11Z,14Z)-N-[(2R)-tetrahydrofuran-2-ylmethyl]icosa-5,8,11,14-tetraenamide
Rattus norvegicus
-
37°C, substrate: anandamide
0.099
(5Z,8Z,11Z,14Z)-N-[(2S)-tetrahydrofuran-2-ylmethyl]icosa-5,8,11,14-tetraenamide
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.091
1,3-benzodioxol-5-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.0051
1-(2-oxo-3-[[4'-(propan-2-yl)biphenyl-4-yl]oxy]propyl)-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000006
1-([1,3]oxazolo[4,5-b]pyridin-2-yl)-6-phenylhexan-1-one
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0012
1-[2-oxo-3-(4-phenoxyphenoxy)propyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0017
1-[2-oxo-3-[4-(2-phenoxyethoxy)phenoxy]propyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0029
1-[2-oxo-3-[4-(2-phenylpropan-2-yl)phenoxy]propyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0019
1-[3-(4-benzylphenoxy)-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00016
1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0064
1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0023
1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0016
1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-sulfonamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0034
1-[3-(biphenyl-3-yloxy)-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00046
1-[3-(biphenyl-4-yloxy)-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00023
1-[3-[(3'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00025
1-[3-[(3'-fluorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.005
1-[3-[(3-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00059
1-[3-[(3-fluorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0074
1-[3-[(3-methoxybiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000464 - 0.00053
1-[3-[(4'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
0.00024
1-[3-[(4'-fluorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00053
1-[3-[(4'-methoxybiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00058
1-[3-[(4'-methylbiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00009
1-[3-[4-(4-fluorophenyl)phenoxy]-2-oxopropyl]indazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0026
1-[3-[4-(decyloxy)phenoxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0034
1-[3-[4-(heptyloxy)phenoxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0035
1-[3-[4-(hexyloxy)phenoxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0018
1-[3-[4-(nonyloxy)phenoxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0022
1-[3-[4-(octyloxy)phenoxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.098
2,2-dimethyl-1,3-dioxolan-4-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.021 - 0.099
2-(5,5-dimethyl-1,3-dioxan-2-yl)ethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
0.00022
3'-carbamoylbiphenyl-3-yl cyclohexylcarbamate
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00531
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N,N-diethylazetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0297
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-ethyl-N-(2-hydroxyethyl)azetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000681
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methyl-N-(2-phenylethyl)azetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.14
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methyl-N-phenylazetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00001
4-(3-phenyl-[1,2,4]thiadiazol-5-yl)piperazine-1-carboxylic acid phenylamide
Rattus norvegicus
-
JNJ-1661010, without preincubation
0.00018
4-(acetylamino)phenyl (4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)acetate
Rattus norvegicus
-
pH 7.4, 37°C
0.0001
4-(acetylamino)phenyl 2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoate
Rattus norvegicus
-
pH 7.4, 37°C
0.058
4-(acetylamino)phenyl 2-[[2-(trifluoromethyl)pyridin-4-yl]amino]pyridine-3-carboxylate
Rattus norvegicus
-
pH 7.4, 37°C
0.0087
4-(acetylamino)phenyl 2-[[3-(trifluoromethyl)phenyl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.3
4-(acetylamino)phenyl 2-[[3-(trifluoromethyl)phenyl]amino]pyridine-3-carboxylate
Rattus norvegicus
-
above, pH 7.4, 37°C
0.064
4-(acetylamino)phenyl 2-{[2-(trifluoromethyl)pyridin-4-yl]amino}benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.0015
4-(acetylamino)phenyl 3-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoate
Rattus norvegicus
-
pH 7.4, 37°C
0.0046
4-(acetylamino)phenyl 3-methyl-4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.047
4-(acetylamino)phenyl 3-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.022
4-(acetylamino)phenyl 4-([[2-(trifluoromethyl)pyridin-4-yl]amino]methyl)benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.031
4-(acetylamino)phenyl 4-chloro-2-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.0027
4-(acetylamino)phenyl 4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.0043
4-(acetylamino)phenyl 5-chloro-2-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.038
4-(acetylamino)phenyl 5-methyl-2-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoate
Rattus norvegicus
-
pH 7.4, 37°C
0.003
4-(acetylamino)phenyl N-(3-methyl-4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoyl)glycinate
Rattus norvegicus
-
pH 7.4, 37°C
0.00087
4-(acetylamino)phenyl N-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]benzoyl)glycinate
Rattus norvegicus
-
pH 7.4, 37°C
0.0026
4-(acetylamino)phenyl N-[(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)acetyl]glycinate
Rattus norvegicus
-
pH 7.4, 37°C
0.00073
4-(acetylamino)phenyl N-[2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanoyl]glycinate
Rattus norvegicus
-
pH 7.4, 37°C
0.000053
4-[3-[4-(decyloxy)phenoxy]-2-oxopropoxy]benzoic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000647
azepan-1-yl[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00263
azetidin-1-yl[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000025
methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraen-1-ylphosphonofluoridate
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00541
N,N-dibenzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00053
N,N-dimethyl-1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-sulfonamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0013
N-(3-methylpyridin-2-yl)-2-(4'-isobutylphenyl)propionamide
Rattus norvegicus
-
pH 7.4, 37°C
0.5
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-(2-hydroxyethyl)azetidine-1-carboxamide
Rattus norvegicus
-
above, pH and temperature not specified in the publication
0.242
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methylazetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.5
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-[2-(dimethylamino)ethyl]azetidine-1-carboxamide
Rattus norvegicus
-
above, pH and temperature not specified in the publication
0.0115
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000094
N-benzyl-3-[(R)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methylazetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00453
N-benzyl-3-[(S)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methylazetidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00075
N-methyl-1-[3-(4-octylphenoxy)-2-oxopropyl]-1H-indole-5-sulfonamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.5
N-tert-butyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
Rattus norvegicus
-
above, pH and temperature not specified in the publication
0.000002 - 0.0000051
N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide
0.011
oxiran-2-ylmethyl (9Z)-octadec-9-enoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.061
oxiran-2-ylmethyl 1,1'-biphenyl-3-carboxylate
Rattus norvegicus
-
37°C, substrate: anandamide
0.035
oxiran-2-ylmethyl 1,1'-biphenyl-4-carboxylate
Rattus norvegicus
-
37°C, substrate: anandamide
0.029
tetrahydro-2H-pyran-2-ylmethyl (9Z)-octadec-9-enoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.0075
tetrahydro-2H-pyran-2-ylmethyl (9Z,12Z)-octadeca-9,12-dienoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.019
tetrahydro-2H-pyran-2-ylmethyl (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.043
tetrahydro-2H-pyran-2-ylmethyl 1,1'-biphenyl-2-carboxylate
Rattus norvegicus
-
37°C, substrate: anandamide
0.018
tetrahydro-2H-pyran-2-ylmethyl 1,1'-biphenyl-3-carboxylate
Rattus norvegicus
-
37°C, substrate: anandamide
0.053
tetrahydro-2H-pyran-2-ylmethyl benzoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.028
[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.017
[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.5
[3-[(2-chlorophenyl)(4-chlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
above, pH and temperature not specified in the publication
0.0184
[3-[(2-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000471
[3-[(2-chloropyridin-3-yl)(3,4-dichlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000713
[3-[(2-chloropyridin-3-yl)(3-methoxyphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000556
[3-[(2-chloropyridin-3-yl)(phenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00542
[3-[(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000375
[3-[(3-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00399
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.5
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-hydroxypiperidin-1-yl)methanone
Rattus norvegicus
-
above, pH and temperature not specified in the publication
0.000505
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-methylpiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.531
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3,4-dihydroisoquinolin-2(1H)-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00524
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.124
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypyrrolidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000161
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-methylpiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000854
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4,4-difluoropiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000388
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-fluoropiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00288
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-hydroxypiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00458
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperazin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000126
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00248
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](morpholin-4-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000447
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00312
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](pyrrolidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00148
[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000937
[3-[(4-chlorophenyl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.5
[3-[(6-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
above, pH and temperature not specified in the publication
0.042
[3-[(S)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000413
[3-[1,3-benzodioxol-5-yl(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000715 - 0.00364
[3-[phenyl(pyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
0.00006
3'-carbamoyl[1,1'-biphenyl]-3-yl cyclohexylcarbamate
Rattus norvegicus
37°C, pH 7.4, assay in brain microsomes, substrate N-(2-hydroxyethyl)-4-pyren-1-ylbutanamide
0.000112
3'-carbamoyl[1,1'-biphenyl]-3-yl cyclohexylcarbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.0000053
4-methoxyphenyl [6-(5-phenyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.00065
4-methoxyphenyl [6-(5-phenyl-2H-tetrazol-2-yl)hexyl]carbamate
Rattus norvegicus
50 mM Tris-HCl, containing 1 mM sodium EDTA, pH 7.4 at 20°C
0.0000043
4-[4-(2,4-difluorophenyl)pyridin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.000074
4-[4-(2,4-difluorophenyl)pyridin-2-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
Rattus norvegicus
pH 9.0, 37°C
0.0024
N-[2-[(3-methylpyridin-2-yl)amino]-2-oxoethyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.027
N-[2-[(3-methylpyridin-2-yl)amino]-2-oxoethyl]-2-(4-[[2-(trifluoromethyl)pyridin-4-yl]amino]phenyl)propanamide
Rattus norvegicus
37°C, pH 7.4
0.0000046
URB597
Rattus norvegicus
pH and temperature not specified in the publication
0.000464
1-[3-[(4'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00053
1-[3-[(4'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.021
2-(5,5-dimethyl-1,3-dioxan-2-yl)ethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.099
2-(5,5-dimethyl-1,3-dioxan-2-yl)ethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.000002
N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide
Rattus norvegicus
-
pH 8.0, 22°C, at 78 nM substrate anandamide
0.0000038
N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide
Rattus norvegicus
-
pH 8.0, 22°C, at 0.01 mM substrate anandamide
0.0000051
N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide
Rattus norvegicus
-
pH 8.0, 22°C, at 0.005 mM substrate anandamide
0.012
oxiran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.019
oxiran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.0082
oxiran-2-ylmethyl (9Z)-hexadec-9-enoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.028
oxiran-2-ylmethyl (9Z)-hexadec-9-enoate
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.0016
oxiran-2-ylmethyl (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.05
oxiran-2-ylmethyl (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.026
tetrahydro-2H-pyran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.051
tetrahydro-2H-pyran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
Rattus norvegicus
-
37°C, substrate: anandamide
0.032
tetrahydro-2H-pyran-2-ylmethyl 1,1'-biphenyl-4-carboxylate
Rattus norvegicus
-
37°C, substrate: anandamide
0.08
tetrahydro-2H-pyran-2-ylmethyl 1,1'-biphenyl-4-carboxylate
Rattus norvegicus
-
37°C, substrate: 2-oleoylglycerol
0.000715
[3-[phenyl(pyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00364
[3-[phenyl(pyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
687528, 695131, 720927, 733500, 733501, 733662, 733794, 734439, 752946, 753277, 753487, 753501, 754287, 754291, 754615
SwissProt
recombinant mutant L192F/F194Y/A377T/S435N/I491V/V495M, a humanized version of the rat FAAH
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
role of FAAH in epithelial cells of the choroid plexus may be to control the concentration of oleamide in the cerebrospinal fluid. FAAH may exert an important regulatory role in shaping the duration and magnitude of the sleep-inducing effect of endogenously or exogenously derived oleamide
-
primary sensory, FAAH is localized in the soma, in small dorsal root ganglion neurons
-
mucosa, urothelium, no FAAH immunoreactivity in other structures of the bladder
additional information
-
culturing does not induce major changes in FAAH expression in primary sensory neurons
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
malfunction
-
effects of FAAH inhibition on bladder function during urodynamics in awake rats, overview
physiological function
additional information
evolution
FAAH is a member of the amidase signature family found in bacteria, archaea and eukaryotes
evolution
fatty acid amide hydrolase is an amidase-signature family member
metabolism
fatty acid amide hydrolase terminates the analgesic and anti-inflammatory effects of endocannabinoids such as anandamide
metabolism
the enzyme has a key role in the control of the cannabinoid signaling, through the hydrolysis of the endocannabinoids anandamide and in some tissues 2-arachidonoylglycerol
physiological function
fatty acid amide hydrolase degrades lipid signaling molecules such as the endogenous cannabinoids anandamide, i.e. N-arachidonyl ethanolamine, and the sleep-inducing substance oleamide, i.e. cis-9-octadecenamide
physiological function
the enzyme degrades and inactivates members of the fatty acid amide family of endogenous signaling lipids, including anandamide and oleamide. Anandamide binds and activates the CB1 and CB2 cannabinoid receptors, the molecular targets of plant-derived (?)-DELTA9-terahydrocannabinol, while oleamide induces physiological sleep and modulates serotonergic systems and GABAergic transmission
physiological function
primary catabolic enzyme for anandamide, an endogenous cannabinoid
physiological function
the enzyme plays a key role in controlling endogenous levels of endocannabinoids
physiological function
-
FAAH is a degradative enzyme for a group of endogenous signaling lipids that includes anandamide, that acts as an endocannabinoid and an endovanilloid by activating cannabinoid and vanilloid type 1 transient receptor potential,TRPV1, receptors, respectively, on dorsal root ganglion sensory neurons. Inhibition of FAAH activity increases anandamide concentrations in nervous tissue and reduces sensory hypersensitivity in animal pain models
physiological function
-
FAAH is the key hydrolytic enzyme for the endogenous cannabinoid receptor ligand anandamide
physiological function
-
endocannabinoid-degrading enzyme fatty acid amide hydrolase. FAAH substrates in the urinary bladder act via local CB2-mediated signals
additional information
the active site is located in the center cavity defined by an atypical Ser-Ser-Lys catalytic triad which comprises the catalytic nucleophile residue Ser241 along with residues Ser217 and Lys142
additional information
the active site of FAAH is characterized by an atypical catalytic triad, consisting of Ser241-Ser217-Ly142, which is capable of hydrolyzing amide and ester bonds at similar rates
additional information
the mammalian enzyme is in the amidase signature (AS) family bearing the unusual Ser-Ser-Lys catalytic triad
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FAAH1_RAT
579
1
63357
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64391
x * 64391, recombinant transmembrane domain-deleted enzyme mutant, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 64391, recombinant transmembrane domain-deleted enzyme mutant, mass spectrometry
oligomer
-
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
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged apo FAAH, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement
recombinant fatty acid amide hydrolase mutant L192F/F194Y/A377T/S435N/I491V/V495M bound to carbamate inhibitor URB597 or inhibitor PF-3845, 25-30 mg/ml protein in 10 mM HEPES, pH 7.0, 500 mM NaCl, 2 mM dithiothreitol, and 0.08% n-undecyl-beta-D-maltoside or 0.1% n-decyl-beta-D-maltoside for inhibitor URB597-enzyme or PF-3845-enzyme conjugate, respectively, supplementation of the FAAHURB597 proteinsample with 1.6% benzyldimethyl(2-dodecyloxyethyl)-ammonium chloride and mixed at a 1:1 proportion with a crystallization buffer containing 30% PEG 400, 100 mM TrisHCl pH 7.5, and 100 mM MgCl2, supplementation of the FAAHPF-3845 protein sample with 1.6% benzyl-dimethyl-dodecyl ammonium bromide and mixed at a 1:1 ratio with a crystallization buffer containing 30% PEG 400, 100 mM 2-(N-morpholino)ethanesulfonate/NaOH, pH 5.5, and 400 mM LiCl, sitting drop vapor diffusion at 14°C, X-ray diffraction structure determination and analysis at 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L192F/F194Y/A377T/S435N/I491V/V495M
generation of a humanized version of the rat FAAH by replacment of six amino acids in the active site of the rat FAAH protein in order to recreate the binding profile of the human enzyme
A487V
-
kcat/Km for nonanoyl p-nitroanilide is 1.3fold higher than wild-type value, kcat/Km for myristoyl p-nitroanilide is 1.5fold lower than wild-type value, kcat/Km for oleoyl p-nitroanilide is 1.4fold lower than wild-type value
D167A
-
mutant enzyme shows 48% of wild-type activity with oleamide as substrate
D237E
-
mutant enzyme shows 12% of wild-type activity with oleamide as substrate
D237N
-
mutant enzyme shows 2.3% of wild-type activity with oleamide as substrate
E143Q
-
mutant enzyme shows 60% of wild-type activity with oleamide as substrate
G489A
-
kcat/Km for nonanoyl p-nitroanilide is 3fold lower than wild-type value, kcat/Km for myristoyl p-nitroanilide is 1.9fold lower than wild-type value, kcat/Km for oleoyl p-nitroanilide is 1.4fold than wild-type value
I491A
-
mutant displays a greatly reduced binding affinity for medium-chain pNA substrates (7-12 carbons), kcat/Km for nonanoyl p-nitroanilide is 8.1fold lower than wild-type value, kcat/Km for myristoyl p-nitroanilide is identical to wild-type value, kcat/Km for oleoyl p-nitroanilide is 2.1fold lower than wild-type value
K142A
K142A/S217A
-
the greater reduction of Ser241 labelling rate in the K142A/S217A double mutant, compared to the K142A and S217A single mutants, suggests that Lys142 and Ser217 cooperate to deprotonate Ser241
K142E
-
mutant enzyme displays severely diminished catalytic activity, but one that now maintains ability of FAAG to react with amides and esters at competitive rates. Mutant enzyme shows an altered pH-rate profile
K142Q
-
mutation abolishes the property of FAAH to degrade amides and esters with equivalent catalytic efficiencies, generating a catalytically compromised enzyme that hydrolyzes esters more than 500fold faster than amides. Mutant enzyme shows an altered pH-rate profile
K255A
-
mutant enzyme shows 17% of wild-type activity with oleamide as substrate
N206A
-
mutant enzyme shows 11% of wild-type activity with oleamide as substrate
R243A
-
mutation decreases the amidase activity of FAAH greater than 100fold without detectably impacting the structural integrity of the enzyme, mutant enzyme shows 24% of the oleoyl ester hydrolysis compared to wild-type enzyme
S217A
S218A
S241A
T257A
-
mutant enzyme shows 65% of wild-type activity with oleamide as substrate
T488A
-
kcat/Km for nonanoyl p-nitroanilide is 2.8fold lower than wild-type value, kcat/Km for myristoyl p-nitroanilide is 1.4fold lower than wild-type value, kcat/Km for oleoyl p-nitroanilide is 1.6fold lower than wild-type value
K142A
-
mutation abolishes the property of FAAH to degrade amides and esters with equivalent catalytic efficiencies, generating a catalytically compromised enzyme that hydrolyzes esters more than 500fold faster than amides. Mutant enzyme shows an altered pH-rate profile
K142A
-
mutation decreases the amidase activity of FAAH greater than 100fold without detectably impacting the structural integrity of the enzyme, mutant enzyme shows 3% of the oleoyl ester hydrolysis compared to wild-type enzyme
K142A
-
the greater reduction of Ser241 labelling rate in the K142A/S217A double mutant, compared to the K142A and S217A single mutants, suggests that Lys142 and Ser217 cooperate to deprotonate Ser241
S217A
-
mutation decreases the amidase activity of FAAH greater than 100fold without detectably impacting the structural integrity of the enzyme, no hydrolysis of oleoyl methyl ester
S217A
-
the greater reduction of Ser241 labelling rate in the K142A/S217A double mutant, compared to the K142A and S217A single mutants, suggests that Lys142 and Ser217 cooperate to deprotonate Ser241
S218A
-
mutation decreases the amidase activity of FAAH greater than 100fold without detectably impacting the structural integrity of the enzyme, mutant enzyme shows 3% of the oleoyl ester hydrolysis compared to wild-type enzyme
S241A
-
mutation decreases the amidase activity of FAAH greater than 100fold without detectably impacting the structural integrity of the enzyme, no hydrolysis of oleoyl methyl ester
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
100 mM Na2CO3 incubation (30 min at 4°C and pH 11.0) destroys the catalytic activity of both wild-type FAAH and FAAH protein lacking the N-terminal transmembrane domain derived from transfected COS-7 cells, whereas the native liver-isolated FAAH is stable to this treatment
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged FAAH from Escherichia coli strain by nickel affinity chromatography
all Escherichia coli expression constructs contained a deletion of the N-terminal transmembrane domain of FAAH. Deletion of this region facilitates its purification from Escherichia coli but had no effect on the enzymatic activity of FAAH
-
recombinantly expressed wild-type FAAH and FAAH protein lacking the N-terminal transmembrane domain
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of mutant L192F/F194Y/A377T/S435N/I491V/V495M in Escherichia coli strain BL21
recombinant expression of transmembrane domain-deleted rat enzyme in Escherichia coli
FAAH is cloned from rat liver plasma membranes and expressed in COS-7 cells
-
FAAH mutants are expressed in the Escherichia coli strain BL21. All Escherichia coli expression constructs contained a deletion of the N-terminal transmembrane domain of FAAH. Deletion of this region facilitates its purification from Escherichia coli but has no effect on the enzymatic activity of FAAH. Some mutants are expressed mainly as inclusion body in Escherichia coli, preventing a detailed analysis of their catalytic function in this system. The expression of FAAH mutants in COS-7 cells provides a system where the majority of these variants can be directly compared
-
wild-type FAAH and FAAH protein lacking the N-terminal transmembrane domain, expression in COS-7 cells and in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
injury to peripheral nerves induces changes in FAAH expression pattern in dorsal root ganglion, while inflammation of peripheral tissues does not induce changes in the FAAH expression pattern, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
FAAH is a promising target for the treatment of several central and peripheral nervous system disorders, such as anxiety, pain and hypertension
medicine
fatty acid amide hydrolase is a promising target for the development of drugs to treat neurological diseases
medicine
inhibition of fatty acid amide hydrolasis is considered a powerful approach to enhance the endocannabinoid signalling and is a potential target for the treatment of neurological disorders such as anxiety or depression, or of inflammatory process
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Patricelli, M.P.; Lashuel, H.A.; Giang, D.K.; Kelly, J.W.; Cravatt, B.F.
Comparative characterization of wild type and transmembrane domain-deleted fatty acid amide hydrolase identification of the transmembrane domain as a site for oligomerization
Biochemistry
37
15177-15187
1998
Rattus norvegicus
Vandevoorde, S.; Fowler, C.J.
Inhibition of fatty acid amide hydrolase and monoacylglycerol lipase by the anandamide uptake inhibitor VDM11: evidence that VDM11 acts as an FAAH substrate
Br. J. Pharmacol.
145
885-893
2005
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Cisneros, J.A.; Vandevoorde, S.; Ortega-Gutierrez, S.; Paris, C.; Fowler, C.J.; Lopez-Rodriguez, M.L.
Structure-activity relationship of a series of inhibitors of monoacylglycerol hydrolysis - comparison with effects upon fatty acid amide hydrolase
J. Med. Chem.
50
5012-5023
2007
Rattus norvegicus
Wei, B.Q.; Mikkelsen, T.S.; McKinney, M.K.; Lander, E.S.; Cravatt, B.F.
A second fatty acid amide hydrolase with variable distribution among placental mammals
J. Biol. Chem.
281
36569-36578
2006
Homo sapiens (O00519), Homo sapiens (Q6GMR7), Homo sapiens, Mus musculus (O08914), Mus musculus, Rattus norvegicus (P97612)
Fowler, C.J.; Jonsson, K.O.; Tiger, G.
Fatty acid amide hydrolase: biochemistry, pharmacology, and therapeutic possibilities for an enzyme hydrolyzing anandamide, 2-arachidonoylglycerol, palmitoylethanolamide, and oleamide
Biochem. Pharmacol.
62
517-26
2001
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Patricelli, M.P.; Cravatt, B.F.
Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism
Biochemistry
38
14125-14130
1999
Rattus norvegicus
Patricelli M.P.; Lovato, M.A.; Cravatt, B.F.
Chemical and mutagenic investigations of fatty acid amide hydrolase: evidence for a family of serine hydrolases with distinct catalytic properties
Biochemistry
38
9804-9812
1999
Rattus norvegicus
Patricelli, M.P.; Cravatt, B.F.
Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase
Biochemistry
40
6107-6115
2001
Rattus norvegicus
Boger, D.L.; Fecik, R.A.; Patterson, J.E.; Miyauchi, H.; Patricelli, M.P.; Cravatt, B.F.
Fatty acid amide hydrolase substrate specificity
Bioorg. Med. Chem. Lett.
10
2613-2616
2000
Rattus norvegicus
Lodola, A.; Mor, M.; Hermann, J.C.; Tarzia, G.; Piomelli, D.; Mulholland, A.J.
QM/MM modelling of oleamide hydrolysis in fatty acid amide hydrolase (FAAH) reveals a new mechanism of nucleophile activation
Chem. Commun. (Camb. )
35
4399-401
2005
Rattus norvegicus
Patricelli, M.P.; Cravatt, B.F.
Clarifying the catalytic roles of conserved residues in the amidase signature family
J. Biol. Chem.
275
19177-19184
2000
Rattus norvegicus
Lang, W.; Qin, C.; Lin, S.; Khanolkar, A.D.; Goutopoulos, A.; Fan, P.; Abouzid, K.; Meng, Z.; Biegel, D.; Makriyannis, A.
Substrate specificity and stereoselectivity of rat brain microsomal anandamide amidohydrolase
J. Med. Chem.
42
898-902
1999
Rattus norvegicus
Romero, F.A.; Du, W.; Hwang, I.; Rayl, T.J.; Kimball, F.S.; Leung, D.; Hoover, H.S.; Apodaca, R.L.; Breitenbucher, J.G.; Cravatt, B.F.; Boger, D.L.J.
Potent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolase
J. Med. Chem.
50
1058-68
2007
Rattus norvegicus
Cravatt, B.F.; Giang, D.K.; Mayfield, S.P.; Boger, D.L.; Lerner, R.A.; Gilula, N.B.
Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
Nature
384
83-87
1996
Rattus norvegicus
Egertova, M.; Cravatt, B.F.; Elphick, M.R.
Fatty acid amide hydrolase expression in rat choroid plexus: possible role in regulation of the sleep-inducing action of oleamide
Neurosci. Lett.
282
13-16
2000
Rattus norvegicus
Giang, D.K.; Cravatt, B.F.
Molecular characterization of human and mouse fatty acid amide hydrolases
Proc. Natl. Acad. Sci. USA
94
2238-2242
1997
Rattus norvegicus, Homo sapiens (O00519), Homo sapiens, Mus musculus (O08914), Mus musculus
Boger, D.L.; Sato, H.; Lerner, A.E.; Hedrick, M.P.; Fecik, R.A.; Miyauchi, H.; Wilkie, G.D.; Austin, B.J.; Patricelli, M.P.; Cravatt, B.F.
Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide
Proc. Natl. Acad. Sci. USA
97
5044-5049
2000
Homo sapiens, Rattus norvegicus
Bracey, M.H.; Hanson, M.A.; Masuda, K.R.; Stevens, R.C.; Cravatt, B.F.
Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling.
Science
298
1793-1796
2002
Rattus norvegicus (P97612)
Karbarz, M.J.; Luo, L.; Chang, L.; Tham, C.S.; Palmer, J.A.; Wilson, S.J.; Wennerholm, M.L.; Brown, S.M.; Scott, B.P.; Apodaca, R.L.; Keith, J.M.; Wu, J.; Breitenbucher, J.G.; Chaplan, S.R.; Webb, M.
Biochemical and biological properties of 4-(3-phenyl-[1,2,4] thiadiazol-5-yl)-piperazine-1-carboxylic acid phenylamide, a mechanism-based inhibitor of fatty acid amide hydrolase
Anesth. Analg.
108
316-329
2009
Rattus norvegicus, Homo sapiens (Q6GMR7), Homo sapiens
Onnis, V.; Congiu, C.; Bjoerklund, E.; Hempel, F.; Soederstroem, E.; Fowler, C.J.
Synthesis and evaluation of paracetamol esters as novel fatty acid amide hydrolase inhibitors
J. Med. Chem.
53
2286-2298
2010
Rattus norvegicus
Lever, I.J.; Robinson, M.; Cibelli, M.; Paule, C.; Santha, P.; Yee, L.; Hunt, S.P.; Cravatt, B.F.; Elphick, M.R.; Nagy, I.; Rice, A.S.
Localization of the endocannabinoid-degrading enzyme fatty acid amide hydrolase in rat dorsal root ganglion cells and its regulation after peripheral nerve injury
J. Neurosci.
29
3766-3780
2009
Rattus norvegicus
Tian, G.; Paschetto, K.A.; Gharahdaghi, F.; Gordon, E.; Wilkins, D.E.; Luo, X.; Scott, C.W.
Mechanism of inhibition of fatty acid amide hydrolase by sulfonamide-containing benzothiazoles: long residence time derived from increased kinetic barrier and not exclusively from thermodynamic potency
Biochemistry
50
6867-6878
2011
Homo sapiens, Rattus norvegicus
Roughley, S.D.; Browne, H.; Macias, A.T.; Benwell, K.; Brooks, T.; D'Alessandro, J.; Daniels, Z.; Dugdale, S.; Francis, G.; Gibbons, B.; Hart, T.; Haymes, T.; Kennett, G.; Lightowler, S.; Matassova, N.; Mansell, H.; Merrett, A.; Misra, A.; Padfield, A.; Parsons, R.; Pratt, R.; Robertson, A.; Simmonite, H.; Tan, K.; Walls, S.B.; Wong, M.
Fatty acid amide hydrolase inhibitors. 3: tetra-substituted azetidine ureas with in vivo activity
Bioorg. Med. Chem. Lett.
22
901-906
2012
Homo sapiens, Rattus norvegicus
Zahov, S.; Drews, A.; Hess, M.; Schulze Elfringhoff, A.; Lehr, M.
1-(3-biaryloxy-2-oxopropyl)indole-5-carboxylic acids and related compounds as dual inhibitors of human cytosolic phospholipase A2alpha and fatty acid amide hydrolase
ChemMedChem
6
544-549
2011
Homo sapiens, Rattus norvegicus
Strittmatter, F.; Gandaglia, G.; Benigni, F.; Bettiga, A.; Rigatti, P.; Montorsi, F.; Gratzke, C.; Stief, C.; Colciago, G.; Hedlund, P.
Expression of fatty acid amide hydrolase (FAAH) in human, mouse, and rat urinary bladder and effects of FAAH inhibition on bladder function in awake rats
Eur. Urol.
61
98-106
2012
Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Mileni, M.; Kamtekar, S.; Wood, D.C.; Benson, T.E.; Cravatt, B.F.; Stevens, R.C.
Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: discovery of a deacylating water molecule and insight into enzyme inactivation
J. Mol. Biol.
400
743-754
2010
Rattus norvegicus (P97612)
Min, X.; Thibault, S.T.; Porter, A.C.; Gustin, D.J.; Carlson, T.J.; Xu, H.; Lindstrom, M.; Xu, G.; Uyeda, C.; Ma, Z.; Li, Y.; Kayser, F.; Walker, N.P.; Wang, Z.
Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH)
Proc. Natl. Acad. Sci. USA
108
7379-7384
2011
Homo sapiens (O00519), Rattus norvegicus (P97612)
Kono, M.; Matsumoto, T.; Imaeda, T.; Kawamura, T.; Fujimoto, S.; Kosugi, Y.; Odani, T.; Shimizu, Y.; Matsui, H.; Shimojo, M.; Kori, M.
Design, synthesis, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase inhibitors
Bioorg. Med. Chem.
22
1468-1478
2014
Homo sapiens (O00519), Rattus norvegicus (P97612), Rattus norvegicus Sprague-Dawley (P97612)
Duncan, K.K.; Otrubova, K.; Boger, D.L.
alpa-Ketoheterocycle inhibitors of fatty acid amide hydrolase: exploration of conformational constraints in the acyl side chain
Bioorg. Med. Chem.
22
2763-2770
2014
Rattus norvegicus (P97612)
Colombano, G.; Albani, C.; Ottonello, G.; Ribeiro, A.; Scarpelli, R.; Tarozzo, G.; Daglian, J.; Jung, K.M.; Piomelli, D.; Bandiera, T.
O-(triazolyl)methyl carbamates as a novel and potent class of fatty acid amide hydrolase (FAAH) inhibitors
ChemMedChem
10
380-395
2015
Homo sapiens (O00519), Homo sapiens, Rattus norvegicus (P97612), Rattus norvegicus SpragueDawley (P97612)
Cipriano, M.; Bjoerklund, E.; Wilson, A.A.; Congiu, C.; Onnis, V.; Fowler, C.J.
Inhibition of fatty acid amide hydrolase and cyclooxygenase by the N-(3-methylpyridin-2-yl)amide derivatives of flurbiprofen and naproxen
Eur. J. Pharmacol.
720
383-390
2013
Rattus norvegicus (P97612)
Alapafuja, S.O.; Nikas, S.P.; Bharathan, I.T.; Shukla, V.G.; Nasr, M.L.; Bowman, A.L.; Zvonok, N.; Li, J.; Shi, X.; Engen, J.R.; Makriyannis, A.
Sulfonyl fluoride inhibitors of fatty acid amide hydrolase
J. Med. Chem.
55
10074-10089
2012
Homo sapiens (O00519), Homo sapiens, Rattus norvegicus (P97612)
Sundermann, T.; Fabian, J.; Hanekamp, W.; Lehr, M.
1-Heteroaryl-3-phenoxypropan-2-ones as inhibitors of cytosolic phospholipase A2alpha and fatty acid amide hydrolase Effect of the replacement of the ether oxygen with sulfur and nitrogen moieties on enzyme inhibition and metabolic stability
Bioorg. Med. Chem.
23
2579-2592
2015
Rattus norvegicus (P97612)
Terwege, T.; Hanekamp, W.; Garzinsky, D.; Koenig, S.; Koch, O.; Lehr, M.
omega-Imidazolyl- and omega-tetrazolylalkylcarbamates as inhibitors of fatty acid amide hydrolase Biological activity and in vitro metabolic stability
ChemMedChem
11
429-443
2016
Rattus norvegicus (P97612)
Deplano, A.; Morgillo, C.M.; Demurtas, M.; Bjoerklund, E.; Cipriano, M.; Svensson, M.; Hashemian, S.; Smaldone, G.; Pedone, E.; Luque, F.J.; Cabiddu, M.G.; Novellino, E.; Fowler, C.J.; Catalanotti, B.; Onnis, V.
Novel propanamides as fatty acid amide hydrolase inhibitors
Eur. J. Med. Chem.
136
523-542
2017
Rattus norvegicus (P97612)
Watabiki, T.; Tsuji, N.; Kiso, T.; Ozawa, T.; Narazaki, F.; Kakimoto, S.
In vitro and in vivo pharmacological characterization of ASP8477 A novel highly selective fatty acid amide hydrolase inhibitor
Eur. J. Pharmacol.
815
42-48
2017
Homo sapiens (B2C6G4), Homo sapiens (O00519), Homo sapiens, Rattus norvegicus (P97612)
Sunduru, N.; Svensson, M.; Cipriano, M.; Marwaha, S.; Andersson, C.D.; Svensson, R.; Fowler, C.J.; Elofsson, M.
N-aryl 2-aryloxyacetamides as a new class of fatty acid amide hydrolase (FAAH) inhibitors
J. Enzyme Inhib. Med. Chem.
32
513-521
2017
Rattus norvegicus (P97612)
Deplano, A.; Cipriano, M.; Moraca, F.; Novellino, E.; Catalanotti, B.; Fowler, C.J.; Onnis, V.
Benzylamides and piperazinoarylamides of ibuprofen as fatty acid amide hydrolase inhibitors
J. Enzyme Inhib. Med. Chem.
34
562-576
2019
Rattus norvegicus (P97612)
EXTERNAL LINKS (specific for EC-Number 3.5.1.99)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
