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Enzyme Nomenclature
Information on EC 3.5.1.99 - fatty acid amide hydrolase
for references in articles please use BRENDA:EC3.5.1.99
Word Map on EC 3.5.1.99
- 3.5.1.99
-
endocannabinoids
- cannabinoids
-
lipase
- pain
- 2-arachidonoylglycerol
- monoacylglycerol
-
rimonabant
-
analgesic
-
vanilloid
-
blockade
-
anxiety
- n-acylethanolamines
- amidase
-
cannabimimetic
- hyperalgesia
-
neuropathic
- carbamate
-
antinociceptive
- n-arachidonoylethanolamine
-
2-arachidonoyl
-
nociceptive
- palmitoylethanolamide
-
anxiolytic
- oleoylethanolamide
- amygdala
- marijuana
- cannabis
-
reward
- delta9-tetrahydrocannabinol
- ethanolamide
- nape-pld
-
psychoactive
- fluorophosphonate
-
sleep-inducing
-
intraplantar
-
neuromodulatory
- pharmacology
- cannabidiol
-
monoacyl
-
anti-allodynic
- drug development
- medicine
- n-oleoylethanolamine
-
dagls
-
periaqueductal
-
arachidonyl
-
nape
- catalepsy
-
anti-hyperalgesic
-
n-acyltransferase
-
capsazepine
-
anxiolytic-like
- monoglyceride
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.5.1.99
-
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RECOMMENDED NAME
GeneOntology No.
fatty acid amide hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anandamide + H2O = arachidonic acid + ethanolamine
-
-
-
-
anandamide + H2O = arachidonic acid + ethanolamine
structure-function relationship and catalytic mechanism, overview
oleamide + H2O = oleic acid + NH3
-
-
-
-
oleamide + H2O = oleic acid + NH3
structure-function relationship and catalytic mechanism, overview
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
153301-19-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
209111, 681315, 690846, 690871, 690872, 690875, 691250, 691760, 692951, 693528, 694331, 694378, 694924, 694928, 695581, 712699, 718908, 719071, 719302
-
-
recombinant mutant L192F/F194Y/A377T/S435N/I491V/V495M, a humanized version of the rat FAAH
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
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
malfunction
-
effects of FAAH inhibition on bladder function during urodynamics in awake rats, overview
malfunction
-
genetic deletion of FAAH is associated with enhanced acute doxorubicin-induced myocardial cell death and decreased survival, mechanism of the doxorubicin-induced myocardial cell death in FAAH+/+ and FAAH-/- mice, overview
malfunction
-
tissue-specific changes in N-acyl ethanolamine congeners and N-acyl taurines metabolism caused by FAAH disruption in central and peripheral tissues, overview
malfunction
-
enzyme inhibition and deficiency causes increased central and peripheral neuronal levels of anandamide and other FAAs producing physiological effects including analgesia, apoptosis in various cancer cells, 12-14 modulation of memory processes, neuroprotection, epilepsy, feeding, and prevention of neurotoxicity of the human amyloid-beta peptide in Alzheimer's disease. Also anti-depressant, anxiolytic, antiinflammatory, anti-hypertensive, gastrointestinal and sleep-inducing effects are observed
malfunction
-
genetic deletion of FAAH is associated with enhanced acute doxorubicin-induced myocardial cell death and decreased survival, mechanism of the doxorubicin-induced myocardial cell death in FAAH+/+ and FAAH-/- mice, overview
-
malfunction
-
effects of FAAH inhibition on bladder function during urodynamics in awake rats, overview
-
metabolism
-
fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury
metabolism
-
fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury
metabolism
-
fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) are key hydrolytic enzymes of the endocannabinoid system
metabolism
-
fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury
-
physiological function
-
importance of FAAH in controlling endogenous anandamide levels in the brain and consequently the importance of FAAH as a regulatory enzyme for key physiological functions. FAAH is one of the main enzymes responsible for terminating the signaling of endocannabinoids in the brain, it has a role in neuropsychiatric disorders
physiological function
-
FAAH is the key hydrolytic enzyme for the endogenous cannabinoid receptor ligand anandamide
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 chief catabolic enzyme regulating the endogenous cannabinoid N-arachidonoylethanolamine, i.e. anandamide
physiological function
-
genetic or pharmacological ablation of FAAH promotes analgesia and anxiolytic effects without disrupting motor coordination
physiological function
-
endocannabinoid-degrading enzyme fatty acid amide hydrolase. FAAH substrates in the urinary bladder act via local CB2-mediated signals
physiological function
-
endocannabinoid-degrading enzyme fatty acid amide hydrolase. FAAH substrates in the urinary bladder act via local CB2-mediated signals
physiological function
-
endocannabinoid-degrading enzyme fatty acid amide hydrolase. FAAH substrates in the urinary bladder act via local CB2-mediated signals
physiological function
-
fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury
physiological function
-
fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury
physiological function
-
fatty acid amide hydrolase is the principal enzyme responsible for anandamide hydrolysis in mammalian tissues and regulates amidated lipid transmitters, including the endocannabinoid anandamide and its N-acyl ethanolamine congeners and transient receptor potential channel agonists N-acyl taurines, in a tissue-specific manner, overview
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
-
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
-
fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury
-
physiological function
-
endocannabinoid-degrading enzyme fatty acid amide hydrolase. FAAH substrates in the urinary bladder act via local CB2-mediated signals
-
additional information
-
anandamide induces enhanced cell death in human cardiomyocytes pretreated by FAAH inhibitor, and enhances sensitivity to reactive oxygen species generation in inflammatory cells of FAAH knockouts
additional information
-
anandamide induces enhanced cell death in human cardiomyocytes pretreated by FAAH inhibitor, and enhances sensitivity to reactive oxygen species generation in inflammatory cells of FAAH knockouts, it triggers concentration-dependent respiratory burst (ROS generation) in neutrophil granulocytes isolated from FAAH+/+ mice
additional information
overexpression of fatty acid amide hydrolase induces early flowering in Arabidopsis thaliana. The FLOWERING LOCUST gene, which plays a major role in regulating flowering time, and one target MADS box transcription factor, SEPATALLA3 (SEP3), are elevated in AtFAAH overexpressors, that also show enhanced NAE hydrolase activity. The early flowering phenotype plants have lower endogenous N-acylethanolamines, NAE, levels in leaves compared to wild-type prior to flowering. The number of rosette leaves and rosette diameter is not affected by altered AtFAAH expression
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 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
additional information
-
the mammalian enzyme is in the amidase signature (AS) family bearing the unusual Ser-Ser-Lys catalytic triad
additional information
-
anandamide induces enhanced cell death in human cardiomyocytes pretreated by FAAH inhibitor, and enhances sensitivity to reactive oxygen species generation in inflammatory cells of FAAH knockouts, it triggers concentration-dependent respiratory burst (ROS generation) in neutrophil granulocytes isolated from FAAH+/+ mice
-
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
-
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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
(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
-
-
?
all-trans-anandamide + H2O
ethanolamine + arachidonic acid
-
all-trans-anandamide is an equally good substrate for rabbit platelet FAAH compared to anandamide
-
-
?
alpha-linolenamide + H2O
? + NH3
-
138% of the activity with oleamide
-
-
?
arachidonyl-7-amino-4-methylcoumarin amide + 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 15–20% of that for anandamide
-
-
?
N-oleoyltaurine + H2O
taurine + oleic acid
4% of the activity with anandamide
-
-
?
palmitoamide + H2O
palmitoic acid + NH3
-
72% of the activity with oleamide
-
-
?
palmitoleamide + H2O
palmitoleic acid + NH3
-
79% of the activity with oleamide
-
-
?
palmitoylethanolamide + H2O
palmitic acid + ethanolamine
-
substrate of FAAH and FAAH-2, the latter shows lower activity than FAAH
-
-
?
stearamide + H2O
stearic acid + NH3
-
69% of the activity with oleamide
-
-
?
2-arachidonoylglycerol + H2O
?
-
FAAH is responsible for approximately one-half of the 2-arachidonoylglycerol hydrolysis occurring in BV-2 cell homogenate
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide, LC-MS/MS analysis
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
substrate of FAAH and FAAH-2, the latter shows lower activity than FAAH
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. N-arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide, LC-MS/MS analysis
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. N-arachidonoylethanolamine
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
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
FAAH-1 plays a primary role in regulating endocannabinoid signaling
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
5% of the activity with oleamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
anandamide hydrolysis in BV-2 cells is entirely attributable to FAAH
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
fatty acid amide hydrolase is a modulator of endogenous signaling compounds affecting sleep (oleamide) and analgesia (anandamide)
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
the enzyme cleaves anandamide and regulates in vivo the magnitude and duration of the signaling induced by this lipid messenger
-
-
?
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
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
-
-
?
arachidonamide + H2O
arachidonic acid + NH3
-
311% of the activity with oleamide
-
-
?
arachidonoyl 7-amido-4-methylcoumarin + H2O
arachidonic acid + 7-amino-4-methylcoumarin
-
-
-
-
?
arachidonoyl 7-amido-4-methylcoumarin + H2O
arachidonic acid + 7-amino-4-methylcoumarin
-
-
-
-
?
arachidonyl-7-amino-4-methylcoumarin amide + H2O
arachidonic acid + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
arachidonyl-7-amino-4-methylcoumarin amide + H2O
arachidonic acid + 7-amino-4-methylcoumarin
-
fluorogenic substrate
-
-
?
myristic amide + H2O
myristic acid + NH3
-
65% of the activity with anandamide
-
-
?
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
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
?
N-oleoylethanolamine + H2O
oleic acid + ethanolamine
23% of the activity with oleamide
-
-
?
N-oleoylethanolamine + H2O
oleic acid + ethanolamine
33% of the activity with anandamide
-
-
?
N-palmitoylethanolamine + H2O
palmitic acid + ethanolamine
12% of the activity with anandamide
-
-
?
N-palmitoylethanolamine + H2O
palmitic acid + ethanolamine
2.3% of the activity with oleamide
-
-
?
oleamide + H2O
oleic acid + NH3
57% of the activity with anandamide
-
-
?
oleamide + H2O
oleic acid + NH3
-
fatty acid amide hydrolase is a modulator of endogenous signaling compounds affecting sleep (oleamide) and analgesia (anandamide)
-
-
?
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
-
33% of the activity with anandamide
-
-
?
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 anandamide
-
-
?
stearic amide + H2O
stearic acid + NH3
-
5.8% of the activity with oleamide
-
-
?
additional information
?
-
-
the substrate specificity of fatty acid ethanolamides decreased with decreasing length, number of double bonds, and lipophilicity of the fatty acid skeleton
-
-
-
additional information
?
-
-
FAAH inactivates anandamide and other bioactive N-acylethanolamines
-
-
-
additional information
?
-
-
the substrate specificity of fatty acid ethanolamides decreased with decreasing length, number of double bonds, and lipophilicity of the fatty acid skeleton
-
-
-
additional information
?
-
-
FAAH is the primary N-arachidonoylethanolamine-degrading enzyme, but it is also capable of hydrolyzing other bioactive N-acylethanolamines, such as N-palmitoylethanolamine, N-oleoylethanolamine and the sleep-inducing lipid 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 Lys–Ser–Ser 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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
2-arachidonoylglycerol + H2O
?
-
FAAH is responsible for approximately one-half of the 2-arachidonoylglycerol hydrolysis occurring in BV-2 cell homogenate
-
-
?
palmitoylethanolamide + H2O
palmitic acid + ethanolamine
-
substrate of FAAH and FAAH-2, the latter shows lower activity than FAAH
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
substrate of FAAH and FAAH-2, the latter shows lower activity than FAAH
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. N-arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. N-arachidonoylethanolamine
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
P97612
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
arachidonic acid + ethanolamine
-
i.e. arachidonoyl ethanolamide
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
O00519, Q6GMR7
FAAH-1 plays a primary role in regulating endocannabinoid signaling
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
anandamide hydrolysis in BV-2 cells is entirely attributable to FAAH
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
fatty acid amide hydrolase is a modulator of endogenous signaling compounds affecting sleep (oleamide) and analgesia (anandamide)
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
-
the enzyme cleaves anandamide and regulates in vivo the magnitude and duration of the signaling induced by this lipid messenger
-
-
?
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
P97612
-
-
-
?
anandamide + H2O
ethanolamine + arachidonic acid
P97612
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
-
-
-
-
?
N-arachidonoylethanolamine + H2O
arachidonic acid + ethanolamine
P97612
-
-
-
?
oleamide + H2O
oleic acid + NH3
-
fatty acid amide hydrolase is a modulator of endogenous signaling compounds affecting sleep (oleamide) and analgesia (anandamide)
-
-
?
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
-
-
?
additional information
?
-
-
FAAH inactivates anandamide and other bioactive N-acylethanolamines
-
-
-
additional information
?
-
-
FAAH is the primary N-arachidonoylethanolamine-degrading enzyme, but it is also capable of hydrolyzing other bioactive N-acylethanolamines, such as N-palmitoylethanolamine, N-oleoylethanolamine and the sleep-inducing lipid oleamide
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-benzhydryltriazol-4-yl)methyl N-cyclohexylcarbamate
-
73% inhibition at 0.1 mM
(1-benzothiophen-6-ylamino)([(E)-[1-(biphenyl-3-yl)ethylidene]amino]oxy)methanone
-
-
(1-benzylpiperidin-4-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
(1H-benzo[d][1,2,3]triazol-1-yl)(4-(3-phenoxybenzyl)-piperazin-1-yl)-methanone
-
-
(1H-benzo[d][1,2,3]triazol-1-yl)(4-(4-phenoxybenzyl)-piperazin-1-yl)-methanone hydrochloride
-
-
(1H-imidazol-1-yl)(4-(4-phenoxy-benzyl)-piperazin-1-yl)-methanone hydrochloride
-
-
(3H-[1,2,3]triazol[4,5-b]pyridin-3-yl)(4-(3-phenoxybenzyl)-piperazin-1-yl)-methanone
-
-
(4-(bis(benzo[d][1,3]dioxol-5-yl)(hydroxy)methyl)-piperidin-1-yl)(1H-1,2,4-triazol-1-yl)methanone
-
-
(4-benzhydrylpiperazin-1-yl)(4-phenyl-1H-imidazol-1-yl)methanone
-
62% activity remaining at 0.01 mM
(4-benzylpiperazin-1-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
(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
-
-
(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)-1-[1,3]oxazolo[4,5-b]pyridin-2-ylicosa-5,8,11,14-tetraen-1-one
-
-
(5Z,8Z,11Z,14Z)-1-[1,3]oxazolo[4,5-c]pyridin-2-ylicosa-5,8,11,14-tetraen-1-one
-
-
(5Z,8Z,11Z,14Z)-1-[1,3]oxazolo[5,4-c]pyridin-2-ylicosa-5,8,11,14-tetraen-1-one
-
-
(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-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide
-
i.e. (5Z,8Z,11Z,14Z)-N-(2-hydroxyethyl)icosa-5,8,11,14-tetraenamide or N-arachidonoylethanolamine, competitive
(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
-
-
(dodecylamino)[[(E)-[1-[3-(thiophen-2-yl)phenyl]ethylidene]amino]oxy]methanone
-
-
(phenylamino)[[(E)-[1-[3-(thiophen-2-yl)phenyl]ethylidene]amino]oxy]methanone
-
-
(phenylamino)[[(E)-[1-[4-(thiophen-2-yl)phenyl]ethylidene]amino]oxy]methanone
-
-
([(E)-[1-(2,2'-bithiophen-5-yl)ethylidene]amino]oxy)(naphthalen-1-ylamino)methanone
-
-
([(E)-[1-(4-cyclohexylphenyl)ethylidene]amino]oxy)(naphthalen-1-ylamino)methanone
-
-
([(E)-[1-(biphenyl-3-yl)ethylidene]amino]oxy)(naphthalen-1-ylamino)methanone
-
-
([(E)-[1-(biphenyl-3-yl)ethylidene]amino]oxy)[(4-fluorophenyl)amino]methanone
-
-
([(E)-[1-(biphenyl-3-yl)ethylidene]amino]oxy)[(4-methoxyphenyl)amino]methanone
-
-
([(E)-[1-(biphenyl-3-yl)ethylidene]amino]oxy)[(5-phenylpentyl)amino]methanone
-
-
([(E)-[1-(biphenyl-4-yl)ethylidene]amino]oxy)(naphthalen-1-ylamino)methanone
-
-
1,1,1,3,3,3-hexafluoropropan-2-yl 4-(3-phenoxybenzyl)piperazine-1-carboxylate
-
-
1-(1-phenyl-1,2,4-triazol-3-yl)methyl N-cyclohexylcarbamate
-
70% inhibition at 0.1 mM
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-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one
1-[(3S)-2-oxo-1-(pent-4-enoyl)azetidin-3-yl]ethyl 3-(1H-indol-3-yl)propanoate
-
-
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-[(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'-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-[4-[bis(1,3-benzodioxol-5-yl)(hydroxy)methyl]piperidin-1-yl]-3,3,3-trifluoro-2-(trifluoromethyl)propan-1-one
-
-
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
-
-
2,2,2-trichloroethyl 4-(bis(benzo[d][1,3]dioxol-5-yl)(hydroxy)methyl)piperidine-1-carboxylate
-
-
2,2-dimethyl-1,3-dioxolan-4-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
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-(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-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-(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
-
-
4-benzhydryl-N-(4-(trifluoromethyl)phenyl)piperazine-1-carboxamide
-
86% activity remaining at 0.01 mM
4-benzhydryl-N-(4-butylphenyl)piperazine-1-carboxamide
-
84% activity remaining at 0.01 mM
4-benzhydryl-N-(4-methoxyphenyl)piperazine-1-carboxamide
-
89% activity remaining at 0.01 mM
4-benzhydryl-N-(4-nitrophenyl)piperazine-1-carboxamide
-
84% activity remaining at 0.01 mM
4-benzhydryl-N-(pyridin-2-yl)piperazine-1-carboxamide
-
87% activity remaining at 0.01 mM
4-benzhydryl-N-(pyridin-3-yl)piperazine-1-carboxamide
-
87% activity remaining at 0.01 mM
4-benzhydryl-N-phenylpiperazine-1-carboxamide
-
88% activity remaining at 0.01 mM
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)(hydroxy)methyl]piperidine-1-carboxylate
-
-
4-nitrophenyl-4-(bis(benzo[d][1,3]dioxol-5-yl)methyl)piperidine-1-carboxylate
-
-
4-[4-(2,4-difluorophenyl)-1,3-thiazol-2-yl]-N-(3,4-dimethyl-1,2-oxazol-5-yl)piperazine-1-carboxamide
5-(4-chlorophenyl)-1-(2,4-dichlorophenyl)-4-methyl-N-morpholin-4-yl-1H-pyrazole-3-carboxamide
-
-
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
-
-
benzyl 4-(dibenzo[d][1,3]dioxol-5-yl(hydroxy)methyl)-piperidine-1-carboxylate
-
-
cyclohexylcarbamic acid 3'-carbamoylbiphenyl-3-yl ester
-
i.e. URB597, attenuates the development of lipopolysaccharide-induced paw edema and reverses lipopolysaccharide-induced hyperalgesia through the respective CB2 and CB1 mechanisms of action. The inhibition is not affected by capsazepine, a transient receptor potential vanilloid type 1 antagonist
ethoxy oleoyl fluorophosphonate
-
irreversible inhibitor, exclusively modifies FAAH at S241
ethyl 4-(3H-[1,2,3]triazolo[4,5-b]pyridin-3-ylcarbonyl)piperazine-1-carboxylate
-
-
methyl 5-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]thiophene-2-carboxylate
-
-
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,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-(3,4-dimethyl-1,2-oxazol-5-yl)-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
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-(phenylcarbamoyl)-3'-[(1E)-N-[(phenylcarbamoyl)oxy]ethanimidoyl]biphenyl-3-carboxamide
-
-
N-(pyridazin-3-yl)-4-(3-[[5-(trifluoromethyl)pyridin-2-yl]oxy]benzylidene)piperidine-1-carboxamide
N-(pyridin-3-yl)-4-(3-[[5-(trifluoromethyl)pyridin-2-yl]oxy]benzyl)piperidine-1-carboxamide
-
-
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-[(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-phenyl-4-(3-phenyl-4,5-dihydro-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
-
-
N-[4-(4-methoxy-1,3-benzothiazol-2-yl)phenyl]-1-(thiophen-2-ylsulfonyl)piperidine-4-carboxamide
piperidin-1-yl[[(E)-[1-[3-(thiophen-2-yl)phenyl]ethylidene]amino]oxy]methanone
-
-
tetrahydro-2H-pyran-2-ylmethyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate
-
-
[(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
-
-
[(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
-
-
[1-[(2-fluoro-3-methoxy-phenyl)methyl]triazol-4-yl]methyl N-cyclohexylcarbamate
-
-
[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(2-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
-
[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-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
[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-[(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](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-[(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
[4-[bis(1,3-benzodioxol-5-yl)methyl]piperidin-1-yl](1H-1,2,4-triazol-1-yl)methanone
-
-
[4-[bis(4-fluorophenyl)methyl]piperazin-1-yl](1H-1,2,4-triazol-1-yl)methanone
-
-
[[(E)-[1-[4-(2,5-dimethyl-1H-pyrrol-1-yl)phenyl]ethylidene]amino]oxy](naphthalen-1-ylamino)methanone
-
-
(1-benzylpiperidin-4-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
(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
-
-
(4-benzylpiperazin-1-yl)[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
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
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-[3-(4-octylphenoxy)-2-oxopropyl]indole-5-carboxylic acid
-
structure-activity relationship, overview
1-[3-[(4'-chlorobiphenyl-4-yl)oxy]-2-oxopropyl]-1H-indole-5-carboxylic acid
-
-
2-(methylamino)-2-oxoethyl [2-[1-(6-methylpyridin-2-yl)piperidin-4-yl]ethyl]carbamate
-
-
2-(methylamino)-2-oxoethyl [2-[1-(6-methylpyridin-2-yl)piperidin-4-yl]ethyl]carbamate
-
-
3'-carbamoylbiphenyl-3-yl cyclohexylcarbamate
-
exerts a combination of anxiolytic-like, anti-depressant-like, and analgesic effects, due to its ability to inhibit FAAH activity in the CNS and peripheral tissues. 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
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
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N,N-diethylazetidine-1-carboxamide
-
-
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-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-(2-phenylethyl)azetidine-1-carboxamide
-
-
3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]-N-methyl-N-phenylazetidine-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)-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
-
4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
-
4-(3-phenyl-[1,2,4]thiadiazol-5-yl)piperazine-1-carboxylic acid phenylamide
-
JNJ-1661010
4-[2-(2,4-difluorophenyl)pyridin-4-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-[2-(2,4-difluorophenyl)pyrimidin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
-
4-[4-(2,3-difluorophenyl)pyrimidin-2-yl]-N-(pyridazin-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)-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)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-(2,4-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-(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
-
analgesic effect of 21d in rat inflammatory pain model, overview
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-[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)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
-
-
4-[6-(2,4-difluorophenyl)pyrimidin-4-yl]-N-(pyridazin-3-yl)piperazine-1-carboxamide
-
-
5-(4-hydroxyphenyl)pentanesulfonyl fluoride
-
i.e. AM3506, irreversible inhibitor for both the rat and the human enzyme, that covalently modifies the enzyme
5-(4-hydroxyphenyl)pentanesulfonyl fluoride
-
; i.e. AM3506, irreversible inhibitor for both the rat and the human enzyme
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide
-
an irreversible covalent inhibitor, binding structure, overview
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide
-
an irreversible covalent inhibitor, binding structure, overview
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-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one
-
reversible inhibitor
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-(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
azepan-1-yl[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
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
-
-
azetidin-1-yl[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl]methanone
-
-
hexadecyl sulfonylfluoride
-
i.e. AM374, is a potent irreversible in vitro and in vivo inhibitor of fatty acid amide hydrolase
hexadecyl sulfonylfluoride
-
i.e. AM374, is a potent in vitro and in vivo inhibitor of fatty acid amide hydrolase
methyl arachidonyl fluorophosphonate
-
MAFP, a potent irreversible FAAH inhibitor
N,N-dibenzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
-
-
N,N-dibenzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidine-1-carboxamide
-
-
N-(3,4-dimethyl-1,2-oxazol-5-yl)-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
-
-
N-(3,4-dimethyl-1,2-oxazol-5-yl)-4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine-1-carboxamide
-
-
N-(pyridazin-3-yl)-4-(3-[[5-(trifluoromethyl)pyridin-2-yl]oxy]benzylidene)piperidine-1-carboxamide
-
-
N-(pyridazin-3-yl)-4-(3-[[5-(trifluoromethyl)pyridin-2-yl]oxy]benzylidene)piperidine-1-carboxamide
-
-
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-(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-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]-N-[2-(dimethylamino)ethyl]azetidine-1-carboxamide
-
-
N-benzyl-3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]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-[(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-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-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
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
oleoyl oxazolopyridine
-
i.e. oloxa, a potent noncompetitive inhibitor, almost complete inhibition at 50 nM
oleoyl oxazolopyridine
-
, i.e. oloxa, a potent noncompetitive inhibitor, almost complete inhibition at 50 nM
PF-3845
crystal structure analysis of enzyme-inhibitor complex. The inhibitor interacts with the catalytic triad and oxyanion hole residues
URB597
-
a carbamate inhibiting FAAH covalently and irreversibly, time-dependent inhibition, overview
URB597
-
a carbamate inhibiting FAAH covalently and irreversibly, time-dependent inhibition, overview
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
[1-[(2,6-difluorophenyl)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-[(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-[(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-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-[(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-[(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-[(3-methoxyphenyl)methyl]triazol-4-yl]methyl N-[[1-[(4-methoxyphenyl)methyl]triazol-4-yl]methyl]carbamate
-
-
[3-[(2-chlorophenyl)(4-chlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
-
[3-[(2-chlorophenyl)(4-chlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
-
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[3-[(2-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(3,4-dichlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(3,4-dichlorophenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(3-methoxyphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(3-methoxyphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(phenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)(phenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(3-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(3-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-hydroxypiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-hydroxypiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-methylpiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](2-methylpiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3,4-dihydroisoquinolin-2(1H)-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3,4-dihydroisoquinolin-2(1H)-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypyrrolidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-hydroxypyrrolidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-methylpiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](3-methylpiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4,4-difluoropiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4,4-difluoropiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-fluoropiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-fluoropiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-hydroxypiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-hydroxypiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperazin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperazin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](4-methylpiperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](morpholin-4-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](morpholin-4-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](pyrrolidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](pyrrolidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
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[3-[(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
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[3-[(4-chlorophenyl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(4-chlorophenyl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(6-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(6-chloropyridin-3-yl)(2-methylphenyl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(S)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[(S)-(4-chlorophenyl)(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[1,3-benzodioxol-5-yl(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[1,3-benzodioxol-5-yl(2-chloropyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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[3-[phenyl(pyridin-3-yl)methoxy]azetidin-1-yl](piperidin-1-yl)methanone
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additional information
-
analysis of the enzyme inhibition by quantum mechanics/molecular mechanics (QM/MM) modelling
-
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
-
a series of oxime carbamates as non-competitive, reversible inhibitors, and show remarkable selectivity for FAAH over the other components of the endocannabinoid system
-
additional information
-
tetra-substituted azetidine ureas with in vivo activity as fatty acid amide hydrolase inhibitors, overview
-
additional information
-
1-(3-biaryloxy-2-oxopropyl)indole-5-carboxylic acids and related compounds can act as dual inhibitors of human 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
-
additional information
-
design, synthesis, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase inhibitors, overview
-
additional information
-
piperazine and piperidine carboxamides and carbamates as enzyme inhibitors, molecular modeling, overview. Diverse leaving groups are tolerated for FAAH inhibitors
-
additional information
-
O-(triazolyl)methyl carbamates as potent fatty acid amide hydrolase inhibitors, overview
-
additional information
-
synthesis of a series of lipophilic ester derivatives of (S)-1-(pent-40-enoyl)-4-(hydroxymethyl)-azetidin-2-one in three steps from (S)-4-(benzyloxycarbonyl)-azetidin-2-one, evaluation as reversible, beta-lactamic inhibitors of endocannabinoid-degrading enzymes, fatty acid amide hydrolase and and monoacylglycerol lipase, docking studies, overview. No inhibition by 1b, 1d, and 1f
-
additional information
-
sulfonyl fluoride inhibitors of fatty acid amide hydrolase, structure-activity relationship, docking and molecular modeling, overview
-
additional information
-
the microglial-specific isozyme is not inhibited by URB597, i.e. 3'-carbamoyl-biphenyl-3-ylcyclohexylcarbamate, and inhibitors of cyclooxygenases, lipooxygenases, and diacylglycerol lipases, overview
-
additional information
-
organophosphorus compound-induced FAAH inhibition and the associated anandamide accumulation may lead to reduced limb mobility as a secondary neurotoxic effect
-
additional information
-
synthesis of 18 aryl analogues of anandamide. In vitro evaluation of inhibitory potency, binding to CB1 and CB2 cannabinoid receptors, and potential as metabolic trapping tracers of 4-methoxyphenethyllinoleoylamide and 4-methoxyphenethylarachidonoylamide, overview
-
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
-
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
-
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
-
design, synthesis, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase inhibitors, 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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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; 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
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
nonanoyl p-nitroanilide
-
pH 9.0, mutant enzyme A487V; pH 9.0, wild-type enzyme
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
0.21
oleoyl p-nitroanilide
-
pH 9.0, mutant enzyme A487V; pH 9.0, mutant enzyme T488A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE