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1-arachidonoylglycerol + H2O
glycerol + arachidonic acid
best substrate
-
-
?
1-decanoyl-rac-glycerol + H2O
glycerol + decanoic acid
-
-
-
?
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol + H2O
?
highest preference
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
2-arachidonoylglycerol + H2O
arachidonoate + glycerol
-
-
-
?
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
2-oleoylglycerol + H2O
oleic acid + glycerol
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferol + butyrate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
7-hydroxycoumarinyl arachidonate + H2O
7-hydroxycoumarin + arachidonate
7-hydroxyresorufinyl arachidonate + H2O
7-hydroxyresorufin + arachidonate
a red fluorogenic substrate, 7-HRA, that is stable in 10% DMSO for at least 36 h at room temperature and for at least 6 months at 4°C, synthesis, overview
-
-
?
arachidonoyl-7-hydroxy-6-methoxy-4-methylcoumarin ester + H2O
arachidonic acid + 7-hydroxy-6-methoxy-4-methylcoumarin
-
-
-
?
prostaglandin D2-glycerol + H2O
?
-
-
-
?
prostaglandin E2-glycerol + H2O
?
-
-
-
?
prostaglandin F2alpha-glycerol + H2O
?
-
-
-
?
umbelliferyl arachidonate + H2O
umbelliferol + arachidonic acid
-
-
-
?
1,3-dihydroxypropan-2-yl 4-pyren-1-ylbutanoate + H2O
pyrenylbutanoic acid + glycerol
-
-
-
-
?
1-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
-
-
-
?
1-capryloyl-rac-glycerol + H2O
glycerol + caprylic acid
-
-
-
-
?
1-decanoyl-rac-glycerol + H2O
glycerol + decanoic acid
-
best substrate
-
-
?
1-lauroyl-rac-glycerol + H2O
glycerol + lauric acid
-
-
-
-
?
1-linoleoylglycerol + H2O
glycerol + linoleic acid
-
-
-
-
?
1-myristoyl-rac-glycerol + H2O
glycerol + myristic acid
-
-
-
-
?
1-palmitoyl-2-lysophosphatidylcholine + H2O
palmitic acid + glycerophosphorylcholine
-
-
-
-
?
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol + H2O
?
-
-
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
-
-
-
?
2-linoleoylglycerol + H2O
glycerol + linoleic acid
-
-
-
-
?
2-monoolein + H2O
?
-
-
-
-
?
2-oleoylglycerol + H2O
glycerol + oleic acid
-
-
-
-
?
2-oleoylglycerol + H2O
oleic acid + glycerol
-
-
-
-
?
2-palmitoylglycerol + H2O
glycerol + palmitic acid
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
7-hydroxycoumarinyl arachidonate
arachidonic acid + 7-hydroxycoumarin
-
-
-
-
?
arachidonoyl-7-hydroxy-6-methoxy-4-methylcoumarin ester + H2O
arachidonic acid + 7-hydroxy-6-methoxy-4-methylcoumarin
-
-
-
-
?
ethyl oleate + H2O
oleic acid + ethanol
-
-
-
-
?
monooleoylglycerol + H2O
oleic acid + glycerol
-
preferred substrate
-
-
?
prostaglandin D2-glycerol + H2O
?
-
-
-
-
?
prostaglandin E2-glycerol + H2O
?
-
-
-
-
?
sn-2-monoolein + H2O
glycerol + oleic acid
-
-
-
-
?
additional information
?
-
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
MGL modulates endocannabinoid signaling in vivo by inactivating 2-arachidonoylglycerol (2-AG), the main endogenous agonist for central CB1 and peripheral CB2 cannabinoid receptors
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
2-arachidonoylglycerol is bound in the tetrahedral intermediate state to Ser122
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
the MGL binding site is a single hydrophobic channel, consisting of an L-shaped main channel with a sub-pocket at the turn. The catalytic S122 of MGL is positioned at the bottom of a single channel
-
-
?
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
-
-
?
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
-
-
-
?
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
-
-
?
7-hydroxycoumarinyl arachidonate + H2O
7-hydroxycoumarin + arachidonate
-
-
-
?
7-hydroxycoumarinyl arachidonate + H2O
7-hydroxycoumarin + arachidonate
fluorescence detection using a fluorogenic probe 1,3-dihydroxypropan-2-yl-4-pyren-1-ylbutanoate
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
-
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
the enzyme is responsible for degradation of 2-arachidonoylglycerol in HeLa cells
-
-
?
additional information
?
-
direct NMR detection of a reversible equilibrium between active and inactive states of human MGL (hMGL) that is slow on the NMR time scale and can be modulated in a controlled manner by pH, temperature, and select point mutations
-
-
?
additional information
?
-
-
direct NMR detection of a reversible equilibrium between active and inactive states of human MGL (hMGL) that is slow on the NMR time scale and can be modulated in a controlled manner by pH, temperature, and select point mutations
-
-
?
additional information
?
-
human monoacylglycerol lipase (MAGL) displays catalytic activity on monoacyl glycerols with medium to long-chain lipophylic moieties such as stearoyl, palmitoyl, oleoyl, and especially arachidonoyl groups. MAGL also demonstrates preference for the hydrolysis of 2-acyl glycerols over their 1(3)-regioisomers. Measurement of MAGL-catalyzed hydrolysis of p-nitrophenyl alkyl esters by monitoring the liberation of p-nitrophenol. Fluorogenic enzyme assay method evaluation, overview
-
-
?
additional information
?
-
-
human monoacylglycerol lipase (MAGL) displays catalytic activity on monoacyl glycerols with medium to long-chain lipophylic moieties such as stearoyl, palmitoyl, oleoyl, and especially arachidonoyl groups. MAGL also demonstrates preference for the hydrolysis of 2-acyl glycerols over their 1(3)-regioisomers. Measurement of MAGL-catalyzed hydrolysis of p-nitrophenyl alkyl esters by monitoring the liberation of p-nitrophenol. Fluorogenic enzyme assay method evaluation, overview
-
-
?
additional information
?
-
usage of a substrate with linoleic acid at the sn-1 position for enzyme activity assays
-
-
?
additional information
?
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-
developmental and nutritional regulation of the enzyme in the intestine, overview
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-
?
additional information
?
-
-
key enzyme responsible for the termination of endocannabinoid signaling with a crucial role in 2-arachidonoylglycerol metabolism, MAGL is unable to mediate anandamide degradation, overview
-
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?
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(3R)-1-(3,4-dimethylphenyl)-5-oxo-N-[(4-oxo-3,4-dihydrophthalazin-1-yl)methyl]pyrrolidine-3-carboxamide
51.85% residual activity at 0.1 mM
(3R)-N-(3,5-dimethylphenyl)-1-[2-(5-fluoro-1H-indol-3-yl)ethyl]-5-oxopyrrolidine-3-carboxamide
18.61% residual activity at 0.1 mM
(3S)-N-(1,3-benzodioxol-4-ylmethyl)-1-[4-[(2-chlorobenzyl)oxy]phenyl]-5-oxopyrrolidine-3-carboxamide
51.09% residual activity at 0.1 mM
(4-(4-chlorobenzoyl)piperidin-1-yl)(4-methoxyphenyl)-methanone
-
(4-[4-chlorobenzoyl]piperidin-1-yl)(4-methoxyphenyl)-methanone
-
12-deacetylsplendidin C
poor inhibition
1H-benzotriazol-1-yl(4-benzylpiperazin-1-yl)methanone
-
1H-benzotriazol-1-yl[4-(4-bromobenzyl)piperazin-1-yl]methanone
-
1H-benzotriazol-1-yl[4-(4-nitrobenzyl)piperazin-1-yl]methanone
-
1H-benzotriazol-1-yl[4-(naphthalen-2-ylmethyl)piperazin-1-yl]methanone
-
1H-benzotriazol-1-yl[4-[(2E)-3-phenylprop-2-en-1-yl]piperazin-1-yl]methanone
-
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-(4-coumaroyl)-beta-D-glucopyranoside
-
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-beta-D-glucopyranoside
the inhibitor is selective for hMAGL over hLDH, modeling of the binding mode in the MAGL active site. The sugar moiety lies in the wide lipophilic cavity of the protein forming lipophilic interactions with L148, L213, L241, and V183, whereas the 4-hydroxyphenyl-ethyl ring lies into the small pocket of the binding site and forms lipophilic interactions with residues Y194 and V270. A high number of H-bonds stabilizes the binding disposition of the compound
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-beta-D-glucopyranoside
-
2-(7-methoxy-2-oxo-2H-chromen-3-yl)-N-(2-methoxyphenyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide
-
2-dehydroxysalvileucanthsin A
poor inhibition
3-[(4S)-1-[2-(5-fluoro-1H-indol-3-yl)ethyl]-2,5-dioxoimidazolidin-4-yl]-N-[(1R,2R)-2-methylcyclohexyl]propanamide
57.6% residual activity at 0.1 mM
5-[(biphenyl-4-yl)methyl]-N,N-dimethyl-2H-tetrazole-2-carboxamide
AM6701, conforms to the L shape of the binding site, contacts with the binding site are similar to those seen with the 2-arachidonoylglycerol docking pose. The close contacts with A164 and K165 are lost as the subpocket is not occupied. Instead the biphenyl moiety, which extends further up the binding pocket, makes additional contacts with A156, T157 and K160, thus AM6701 is a non-selective inhibitor
benzyl [4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)-2-methylphenyl]carbamate
5.12% residual activity at 0.1 mM
jewenol A
reversible inhibitor, catalytic site binding structure, overview
LY2183240
is less potent than JZL184
methyl arachidonyl fluorophosphonate
N-arachidonylmaleimide
Cys201 is the crucial residue in MAGL inhibition by N-arachidonylmaleimide
N-[3-(4-fluorophenyl)-6-oxopyrazolo[5,1-c]pyrido[4,3-e][1,2,4]triazin-7(6H)-yl]-2-(naphthalen-2-yloxy)acetamide
72.3% residual activity at 0.1 mM
N-[4-(1,3-benzothiazol-2-yl)phenyl]-2-(1H-benzotriazol-1-yl)acetamide
14.28% residual activity at 0.1 mM
phenylmethylsulfonyl fluoride
PMSF is able to produce an irreversible MAGL-PMSF adduct and hydrofluoric acid (HF), by specifically binding to the hydroxyl group of the serine residue in the active site of the serine protease, thereby inhibiting its enzymatic activity
pinoresinol 4-O-beta-D-glucopyranoside
-
pseudorosmaricin
poor inhibition
[4-[bis(1,3-benzodioxol-5-yl)methyl]-1-piperidinyl](1H-1,2,4-triazol-1-yl)methanone
a highly potent selective inhibitor
(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
-
16% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3R,4R)-3-[1(R)-(3-phenylpropanoyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3R,4R)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3R,4R)-3-[1(R)-(biphenylacetyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
1-(3-phenylpropanoyl)-(3S)-3-[1(R)-(3-phenylpropanoyloxy)-ethyl]-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3S)-3-[1(R)-(5-phenylpentanoyloxy)-ethyl]-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
-
31% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(4-phenylbutanoyl)-(3R,4R)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(4-phenylbutanoyl)-(3R,4R)-3-[1(R)-hydroxyethyl]-4-(acetoxy)-azetidin-2-one
-
61% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(4-phenylbutanoyl)-(3S)-3-[1(R)-(3-phenylpropanoyloxy)-ethyl]-azetidin-2-one
-
54% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(4-phenylbutanoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(4-phenylbutanoyl)-(3S)-3-[1(R)-(5-phenylpentanoyloxy)-ethyl]-azetidin-2-one
-
59% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(5-phenylpentanoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
-
39% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(5-phenylpentanoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
-
25% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(hexa-5-enoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
-
85% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(hexa-5-enoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
-
67% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3R,4R)-3-[1(R)-(pent-4-enoyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
-
99% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3R,4R)-3-[1(R)-hydroxyethyl]-4-(acetoxy)-azetidin-2-one
1-(pent-4-enoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
-
89% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
-
91% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3S)-3-[1(R)-(hexa-5-enoyloxy)-ethyl]-azetidin-2-one
-
8% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3S)-3-[1(R)-(pent-4-enoyloxy)-ethyl]-azetidin-2-one
-
99% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3S)-3-[1(R)-hydroxyethyl]-azetidin-2-one
-
89% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
15-deoxy-DELTA12,14-prostaglandin J2
-
-
2-arachidonoylglycerol
-
-
4-chloromercuribenzoic acid
-
-
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)hydroxymethyl]piperidine-1-carboxylate
-
JZL184
6-methyl-2-p-tolylamino-benzo[d] [1,3]oxazin-4-one
-
i.e. URB754
AM6580
-
irreversible inhibitor, i.e. [4-(9H-fluoren-9-yl)-piperazin-1-yl][1,2,3]triazolo[4,5-b]pyridin-1-ylmethanone
arachidonoyltrifluoromethyl ketone
-
i.e. ATFMK
arachidonoyltrifluoromethylketone
-
-
benzylphenylcarbamate
-
-
biphenyl-3-yl-carbamic acid cyclohexyl ester
-
i.e. URB602
Diethyl p-nitrophenyl phosphate
-
-
diisopropyl fluorophosphate
-
-
isopropyldodecylfluorophosphonate
-
-
JJKK-048
-
i.e. 4-[bis-(benzo[d][1,3]dioxol-5-yl)methyl]-piperidin-1-yl}(1H-1,2,4-triazol-1-yl)methanone
methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14- tetraenylphosphonofluoridate
-
completely inhibits 4-nitophenyl acetate hydrolysis by pure human MGL at 0.1 mM
methyl arachidonyl fluorophosphonate
methylarachidonoylfluorophosphonate
-
-
N-arachidonoyl dopamine
-
-
N-arachidonyl maleimide
-
potent irreversible inhibitor of MAGL, inhibits in a dose-dependent manner
N-arachidonylmaleimide
-
-
N-benzoylthiocarbamic cyclohexylethyl ester
-
-
NaCl
-
1 M, 63% loss of activity
phenylmethylsulfonyl fluoride
-
inhibits MGL only at very high concentrations
[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3-yl)-2-methylphenyl]carbamic acid benzyl ester
-
CAY10499
JZL184
-
JZL184
is more potent than LY2183240. The p-nitrophenyl group fits better in the MAGL cavity than the corresponding substituent of LY2183240
JZL184
MGL-selective inhibitor, represents a ligand with increased steric bulk over AM6701 and 2-arachidonoylglycerol. Extra bulk fills the binding site more completely and one 1,3-benzodioxole moiety makes additional contacts with the lid region of MGL. There is also a weak hydrogen bond from N195 to the p-nitro substituent
methyl arachidonyl fluorophosphonate
-
methyl arachidonyl fluorophosphonate
irreversible active-site inhibitor of monoglyceride lipase
1-(3-phenylpropanoyl)-(3R,4R)-3-[1(R)-(biphenylacetyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
-
100% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(3-phenylpropanoyl)-(3R,4R)-3-[1(R)-(biphenylacetyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
-
66% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3R,4R)-3-[1(R)-hydroxyethyl]-4-(acetoxy)-azetidin-2-one
-
16% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
1-(pent-4-enoyl)-(3R,4R)-3-[1(R)-hydroxyethyl]-4-(acetoxy)-azetidin-2-one
-
8% inhibition, with 0.1 mM of inhibitor, at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
AM6701
-
5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetrazole-2-carboxamide
AM6701
-
MGL inhibition by AM6701 involves a covalent interaction resulting in the enzyme's rapid, selective carbamoylation at its catalytic serine nucleophile (Ser122)
AM6701
-
slowly reversible inhibition, i.e. 5-((biphenyl-4-yl)methyl)-N,N-dimethyl-2H-tetra-zole-2-carboxamide
Disulfiram
-
-
Disulfiram
-
i.e. tetraethylthiuram disulfide, a compound used to treat alcoholism, inhibition likely through an interaction with cysteine residues Cys208 and/or Cys242, the inhibition is reversible by DTT
JZL184
-
-
JZL184
-
irreversible inhibitor
JZL184
-
time-dependent inhibitor
JZL184
-
i.e. 4-nitrophenyl 4-(dibenzo[d][1,3]dioxol-5-yl(hydroxy)methyl)piperidine-1-carboxylate
methyl arachidonyl fluorophosphonate
-
i.e. MAFP
methyl arachidonyl fluorophosphonate
-
MAFP
N-arachidonoylmaleimide
-
-
N-arachidonoylmaleimide
-
irreversible inhibition
N-arachidonoylmaleimide
-
inhibits MGL through partial enzyme alkylation at Cys208 and/or Cys242 (Cys242 being favored)
URB602
-
-
URB602
-
specific inhibitor of MAGL, inhibits in a dose-dependent manner
additional information
diterpenes from Salvia pseudorosmarinus and their activity as inhibitors of monoacylglycerol lipase (MAGL), NMR structure analysis, molecular docking into the catalytic site of the enzyme, overview. No effect by DTT at 0.1 mM and by galloflavin
-
additional information
phenylethanoid glycosides isolated from the n-butanol extract of Cistanche phelypaea aerial parts (collected in March 2012 in the southwest of Algeria) show activity as inhibitors of monoacylglycerol lipase, structure determinations by spectroscopic analyses, including 1D and 2D NMR, and HRESIMS experiments, docking study, overview. No inhibition by galloflavin, apigenin 7-O-beta-D-glucuronopyranoside, and 2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-(4-coumaroyl)-beta-D-glucopyranoside
-
additional information
structure-based MGL inhibitor design
-
additional information
-
structure-based MGL inhibitor design
-
additional information
-
immunodepletion of the enzyme leads to 50% reduced activity
-
additional information
-
inhibitor screening, molecular docking and modeling, no inhibition of MGL by fatty acid amide hydrolase inhibitors, overview
-
additional information
-
no inhibition by URB754
-
additional information
-
not inhibited by CAY10433, WWL70, and URB602
-
additional information
-
1-(4-phenylbutanoyl)-(3S)-3-[1(R)-hydroxyethyl]-azetidin-2-one, 1-(5-phenylpentanoyl)-(3S)-3-[1(R)-hydroxyethyl]-azetidin-2-one, 1-(hexa-5-enoyl)-(3S)-3-[1(R)-hydroxyethyl]-azetidin-2-one and 1-(4-phenylbutanoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one do not inhibit
-
additional information
-
URB754 does not inhibit MAGL activity at concentrations up to 0.100 mM. Assay buffer alone or heat-denatured MAGL protein has no significant activity against 7-hydroxycoumarinyl-arachidonate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Acute Lung Injury
Monoacylglycerol lipase (MAGL) inhibition attenuates acute lung injury in mice.
Acute Lung Injury
The monoacylglycerol lipase inhibitor JZL184 decreases inflammatory response in skeletal muscle contusion in rats.
acylglycerol lipase deficiency
Monoacylglycerol lipase deficiency affects diet-induced obesity, fat absorption, and feeding behavior in CB1 cannabinoid receptor-deficient mice.
acylglycerol lipase deficiency
Monoacylglycerol lipase deficiency in the tumor microenvironment slows tumor growth in non-small cell lung cancer.
acylglycerol lipase deficiency
Monoglyceride lipase deficiency affects hepatic cholesterol metabolism and lipid-dependent gut transit in ApoE-/- mice.
acylglycerol lipase deficiency
Monoglyceride lipase deficiency causes desensitization of intestinal cannabinoid receptor type 1 and increased colonic ?-opioid receptor sensitivity.
acylglycerol lipase deficiency
Monoglyceride lipase deficiency modulates endocannabinoid signaling and improves plaque stability in ApoE-knockout mice.
Adenocarcinoma of Lung
Monoacylglycerol Lipase Knockdown Inhibits Cell Proliferation and Metastasis in Lung Adenocarcinoma.
Adenocarcinoma of Lung
Monoglyceride lipase gene knockout in mice leads to increased incidence of lung adenocarcinoma.
Adenoma
Prdm5 suppresses Apc(Min)-driven intestinal adenomas and regulates monoacylglycerol lipase expression.
Alzheimer Disease
Alleviation of Neuropathology by Inhibition of Monoacylglycerol Lipase in APP Transgenic Mice Lacking CB2 Receptors.
Alzheimer Disease
Dysregulated expression of monoacylglycerol lipase is a marker for anti-diabetic drug metformin-targeted therapy to correct impaired neurogenesis and spatial memory in Alzheimer's disease.
Alzheimer Disease
Molecular reorganization of endocannabinoid signalling in Alzheimer's disease.
Alzheimer Disease
Monoacylglycerol lipase is a therapeutic target for Alzheimer's disease.
Arthralgia
Combatting joint pain and inflammation by dual inhibition of monoacylglycerol lipase and cyclooxygenase-2 in a rat model of osteoarthritis.
Arthritis
Monoacylglycerol Lipase Inhibition Using JZL184 Attenuates Paw Inflammation and Functional Deficits in a Mouse Model of Inflammatory Arthritis.
Arthritis
Rescue of Impaired mGluR5-Driven Endocannabinoid Signaling Restores Prefrontal Cortical Output to Inhibit Pain in Arthritic Rats.
Atherosclerosis
Deficiency of Monoacylglycerol Lipase Enhances IgM Plasma Levels and Limits Atherogenesis in a CB2-Dependent Manner.
Brain Injuries
Pretreatment with the monoacylglycerol lipase inhibitor URB602 protects from the long-term consequences of a neonatal hypoxic-ischemic brain injury in rats.
Breast Neoplasms
Comparative Proteome Analysis of Breast Cancer Tissues Highlights the Importance of Glycerol-3-phosphate Dehydrogenase 1 and Monoacylglycerol Lipase in Breast Cancer Metabolism.
Breast Neoplasms
Fatty acid-binding protein 5 (FABP5) promotes lipolysis of lipid droplets, de novo fatty acid (FA) synthesis and activation of nuclear factor-kappa B (NF-?B) signaling in cancer cells.
Breast Neoplasms
Identification of genes with altered expression in medullary breast cancer vs. ductal breast cancer and normal breast epithelia.
Carcinogenesis
Chewing the fat on tumor cell metabolism.
Carcinogenesis
Effect of monoacylglycerol lipase on the tumor growth in endometrial cancer.
Carcinoma, Hepatocellular
Circulating prostaglandin E2: a novel potential prognostic biomarker in patients with hepatocellular carcinoma.
Carcinoma, Hepatocellular
KLF4 suppresses the migration of hepatocellular carcinoma by transcriptionally upregulating monoglyceride lipase.
Carcinoma, Hepatocellular
Monoacylglycerol lipase promotes progression of hepatocellular carcinoma via NF-?B-mediated epithelial-mesenchymal transition.
Carcinoma, Hepatocellular
Monoacylglycerol Lipase: A Novel Potential Therapeutic Target and Prognostic Indicator for Hepatocellular Carcinoma.
Carcinoma, Hepatocellular
The ménage à trois of autophagy, lipid droplets and liver disease.
Carcinoma, Hepatocellular
[Monoacylglycerol lipase high expression as an independent indicator of survival for patients with hepatocellular carcinoma].
Carcinoma, Non-Small-Cell Lung
Monoacylglycerol lipase deficiency in the tumor microenvironment slows tumor growth in non-small cell lung cancer.
Cerebral Cortical Thinning
Brain structural changes in cannabis dependence: association with MAGL.
Cholangitis, Sclerosing
Monoacylglycerol lipase inhibition protects from liver injury in mouse models of sclerosing cholangitis.
Colitis
Increasing endogenous 2-arachidonoylglycerol levels counteracts colitis and related systemic inflammation.
Colitis
Manipulation of the Endocannabinoid System in Colitis: A Comprehensive Review.
Colitis
The monoacylglycerol lipase inhibitor JZL184 decreases inflammatory response in skeletal muscle contusion in rats.
Colonic Neoplasms
Monoacylglycerol lipase regulates cannabinoid receptor 2-dependent macrophage activation and cancer progression.
Colonic Neoplasms
Prdm5 suppresses Apc(Min)-driven intestinal adenomas and regulates monoacylglycerol lipase expression.
Colorectal Neoplasms
Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer.
Colorectal Neoplasms
Monoacylglycerol lipase inhibitor JZL184 regulates apoptosis and migration of colorectal cancer cells.
Colorectal Neoplasms
Potential tumor-suppressive role of monoglyceride lipase in human colorectal cancer.
Colorectal Neoplasms
Targeting triglyceride metabolism for colorectal cancer prevention and therapy.
Congenital Abnormalities
Anticholinesterase insecticide action at the murine male reproductive system.
Cystitis, Interstitial
Monoacylglycerol lipase inhibition as potential treatment for interstitial cystitis.
Demyelinating Diseases
Blockade of monoacylglycerol lipase inhibits oligodendrocyte excitotoxicity and prevents demyelination in vivo.
Down Syndrome
Monoacylglycerol lipase inhibitor JZL184 improves behavior and neural properties in Ts65Dn mice, a model of down syndrome.
Encephalomyelitis
2-Arachidonoylglycerol Reduces Proteoglycans and Enhances Remyelination in a Progressive Model of Demyelination.
Endometrial Neoplasms
Effect of monoacylglycerol lipase on the tumor growth in endometrial cancer.
Endometrial Neoplasms
The levels of the endocannabinoid receptor CB2 and its ligand 2-arachidonoylglycerol are elevated in endometrial carcinoma.
Enteritis
[Monoglyceride lipase insufficiency of the small intestine in chronic enteritis]
Epilepsy
Inhibition of monoacylglycerol lipase mediates a cannabinoid 1-receptor dependent delay of kindling progression in mice.
Epilepsy, Temporal Lobe
Inhibition of monoacylglycerol lipase mediates a cannabinoid 1-receptor dependent delay of kindling progression in mice.
Fatty Liver
?/? Hydrolase Domain-containing 6 (ABHD6) Degrades the Late Endosomal/Lysosomal Lipid Bis(monoacylglycero)phosphate.
Fatty Liver
Absence of Adiponutrin (PNPLA3) and Monoacylglycerol Lipase Synergistically Increases Weight Gain and Aggravates Steatohepatitis in Mice.
Fatty Liver
The ménage à trois of autophagy, lipid droplets and liver disease.
Glaucoma
Synthesis and evaluation of potent and selective MGL inhibitors as a glaucoma treatment.
Glioma
Lack of selectivity of URB602 for 2-oleoylglycerol compared to anandamide hydrolysis in vitro.
Head Injuries, Closed
Inhibition of monoacylglycerol lipase prevents chronic traumatic encephalopathy-like neuropathology in a mouse model of repetitive mild closed head injury.
Heart Arrest
Monoacylglycerol Lipase Inactivation by Using URB602 Mitigates Myocardial Damage in a Rat Model of Cardiac Arrest.
Heart Arrest
Monoacylglycerol Lipase Inactivation by Using URB602 Mitigates Myocardial Damage in a Rat Model of Cardiac Arrest: Erratum.
Hepatitis
Endogenous and postheparin monoglyceride hydrolase in plasma of patients with acute virus hepatitis.
Hepatitis C
Profiling of MicroRNA Targets Using Activity-Based Protein Profiling: Linking Enzyme Activity to MicroRNA-185 Function.
Hyperalgesia
Endogenous opioid and cannabinoid systems modulate the muscle pain: A pharmacological study into the peripheral site.
Hyperalgesia
Fatty Acid Amide Hydrolase and Monoacylglycerol Lipase Inhibitors Produce Anti-Allodynic Effects in Mice Through Distinct Cannabinoid Receptor Mechanisms.
Hyperalgesia
Monoacylglycerol lipase inhibitors reverse paclitaxel-induced nociceptive behavior and proinflammatory markers in a mouse model of chemotherapy-induced neuropathy.
Hyperalgesia
The monoacylglycerol lipase inhibitor JZL184 suppresses inflammatory pain in the mouse carrageenan model.
Hyperalgesia
Therapeutic potential of inhibitors of endocannabinoid degradation for the treatment of stress-related hyperalgesia in an animal model of chronic pain.
Hyperlipidemias
Post-heparin plasma hepatic triglyceride lipase and monoglyceride hydrolase activities in hyperlipemia induced by a sucrose rich diet.
Hyperlipidemias
[Post-heparin lipolytic activity. (III). Lipoprotein lipase and monoglyceride hydrolase activities on hyperlipemia and the organs responsible for their biosynthesis]
Hyperlipoproteinemias
[Activity of endogenous monoglyceride hydrolase in healthy subjects and patients with type IV Fredricksoln's hyperlipoproteinemia]
Hypertension
Crosstalk between liver antioxidant and the endocannabinoid systems after chronic administration of the FAAH inhibitor, URB597, to hypertensive rats.
Hypertriglyceridemia
Effects of tiadenol and clofibrate on plasma post heparin lipolytic hepatic, extrahepatic and monoglyceride hydrolase activities in rats with hypertriglyceridemia induced by a sucrose rich diet.
Infarction, Middle Cerebral Artery
Monoacylglycerol lipase inhibitor, JZL-184, confers neuroprotection in the mice middle cerebral artery occlusion model of stroke.
Infections
Effects of the monoacylglycerol lipase inhibitor JZL184 on chickens infected with avian pathogenic Escherichia coli O78: A preliminary pharmacokinetic and infection study.
Infections
Hemolytic phospholipase Rv0183 of Mycobacterium tuberculosis induces inflammatory response and apoptosis in alveolar macrophage RAW264.7 cells.
Infertility, Male
Tapetal Expression of BnaC.MAGL8.a Causes Male Sterility in Arabidopsis.
Liver Diseases
Inhibition of monoacylglycerol lipase for the treatment of liver disease: tempting but still playing with fire.
Liver Diseases
Monoacylglycerol lipase reprograms lipid precursors signaling in liver disease.
Liver Diseases
The ménage à trois of autophagy, lipid droplets and liver disease.
Liver Diseases
[Clinical experience with a new method for the determination of monoglyceride lipase (author's transl)]
Liver Neoplasms
Aberrant lipid metabolism as a therapeutic target in liver cancer.
Liver Neoplasms
[Effect of monoacylglycerol lipase with proliferation of MHCC97H human liver cancer cells in vivo].
Lung Neoplasms
Monoacylglycerol lipase deficiency in the tumor microenvironment slows tumor growth in non-small cell lung cancer.
Lung Neoplasms
The Monoacylglycerol Lipase Inhibitor JZL184 Inhibits Lung Cancer Cell Invasion and Metastasis via the CB1 Cannabinoid Receptor.
Melanoma
Expression of monoacylglycerol lipase as a marker of tumour invasion and progression in malignant melanoma.
Migraine Disorders
Distinct Activity of Endocannabinoid-Hydrolyzing Enzymes MAGL and FAAH in Key Regions of Peripheral and Central Nervous System Implicated in Migraine.
Migraine Disorders
Emerging Role of (Endo)Cannabinoids in Migraine.
Migraine Disorders
Inhibition of FAAH reduces nitroglycerin-induced migraine-like pain and trigeminal neuronal hyperactivity in mice.
Migraine Disorders
Inhibition of monoacylglycerol lipase: Another signalling pathway for potential therapeutic targets in migraine?
Migraine Disorders
P007. Inhibition of monoacylglycerol lipase activity modulates the activation of brain structures relevant for migraine pathogenesis.
Multiple Myeloma
JZL184, A Monoacylglycerol Lipase Inhibitor, Induces Bone Loss in a Multiple Myeloma Model of Immunocompetent Mice.
Multiple Sclerosis
A reversible and selective inhibitor of monoacylglycerol lipase ameliorates multiple sclerosis.
Myocardial Infarction
2-arachidonoylglycerol mobilizes myeloid cells and worsens heart function after acute myocardial infarction.
Nasopharyngeal Carcinoma
Monoacylglycerol lipase promotes metastases in nasopharyngeal carcinoma.
Neoplasm Metastasis
Expression of monoacylglycerol lipase as a marker of tumour invasion and progression in malignant melanoma.
Neoplasm Metastasis
Monoacylglycerol Lipase Knockdown Inhibits Cell Proliferation and Metastasis in Lung Adenocarcinoma.
Neoplasm Metastasis
Monoacylglycerol lipase promotes metastases in nasopharyngeal carcinoma.
Neoplasm Metastasis
The Monoacylglycerol Lipase Inhibitor JZL184 Inhibits Lung Cancer Cell Invasion and Metastasis via the CB1 Cannabinoid Receptor.
Neoplasms
?-Quinazolinonylalkyl aryl ureas as reversible inhibitors of monoacylglycerol lipase.
Neoplasms
Astroglial monoacylglycerol lipase controls mutant huntingtin-induced damage of striatal neurons.
Neoplasms
Chemical approaches to therapeutically target the metabolism and signaling of the endocannabinoid 2-AG and eicosanoids.
Neoplasms
Computationally driven discovery of phenyl(piperazin-1-yl)methanone derivatives as reversible monoacylglycerol lipase (MAGL) inhibitors.
Neoplasms
Development of thiazole-5-carboxylate derivatives as selective inhibition of monoacylglycerol lipase as a target in Cancer.
Neoplasms
Effect of monoacylglycerol lipase on the tumor growth in endometrial cancer.
Neoplasms
Endocannabinoids as endometrial inflammatory markers in lactating Holstein cows.
Neoplasms
Expression of monoacylglycerol lipase as a marker of tumour invasion and progression in malignant melanoma.
Neoplasms
Identification of genes with altered expression in medullary breast cancer vs. ductal breast cancer and normal breast epithelia.
Neoplasms
JZL184, A Monoacylglycerol Lipase Inhibitor, Induces Bone Loss in a Multiple Myeloma Model of Immunocompetent Mice.
Neoplasms
Modulation of the Endocannabinoid System as a Potential Anticancer Strategy.
Neoplasms
Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer.
Neoplasms
Monoacylglycerol lipase deficiency in the tumor microenvironment slows tumor growth in non-small cell lung cancer.
Neoplasms
Monoacylglycerol lipase inhibitors: modulators for lipid metabolism in cancer malignancy, neurological and metabolic disorders.
Neoplasms
Monoacylglycerol Lipase Knockdown Inhibits Cell Proliferation and Metastasis in Lung Adenocarcinoma.
Neoplasms
Monoacylglycerol lipase promotes progression of hepatocellular carcinoma via NF-?B-mediated epithelial-mesenchymal transition.
Neoplasms
Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis.
Neoplasms
Monoacylglycerol lipase regulates cannabinoid receptor 2-dependent macrophage activation and cancer progression.
Neoplasms
Monoacylglycerol Lipase: A Novel Potential Therapeutic Target and Prognostic Indicator for Hepatocellular Carcinoma.
Neoplasms
Monoglyceride lipase mediates tumor-suppressive effects by promoting degradation of X-linked inhibitor of apoptosis protein.
Neoplasms
Monoglyceride lipase: Structure and inhibitors.
Neoplasms
Pharmacological inhibition of MAGL attenuates experimental colon carcinogenesis.
Neoplasms
Potential tumor-suppressive role of monoglyceride lipase in human colorectal cancer.
Neoplasms
Structural Optimization of 4-Chlorobenzoylpiperidine Derivatives for the Development of Potent, Reversible, and Selective Monoacylglycerol Lipase (MAGL) Inhibitors.
Neoplasms
The Endocannabinoid System Alleviates Pain in a Murine Model of Cancer-Induced Bone Pain.
Neoplasms
The Role of Monoacylglycerol Lipase (MAGL) in the Cancer Progress.
Nervous System Diseases
Activity-Based Protein Profiling Delivers Selective Drug Candidate ABX-1431, a Monoacylglycerol Lipase Inhibitor, To Control Lipid Metabolism in Neurological Disorders.
Nervous System Diseases
Identification of ABX-1431, a Selective Inhibitor of Monoacylglycerol Lipase and Clinical Candidate for Treatment of Neurological Disorders.
Neuralgia
Combined inhibition of monoacylglycerol lipase and cyclooxygenases synergistically reduces neuropathic pain in mice.
Neuralgia
Inhibition of 2-arachydonoylgycerol degradation attenuates orofacial neuropathic pain in trigeminal nerve-injured mice.
Neuralgia
Systematic review and meta-analysis of cannabinoids, cannabis-based medicines, and endocannabinoid system modulators tested for antinociceptive effects in animal models of injury-related or pathological persistent pain.
Neuralgia
The Endogenous Cannabinoid System: A Budding Source of Targets for Treating Inflammatory and Neuropathic Pain.
Neuralgia
The Selective Monoacylglycerol Lipase Inhibitor MJN110 Produces Opioid-Sparing Effects in a Mouse Neuropathic Pain Model.
Neuroblastoma
Low mRNA expression and activity of monoacylglycerol lipase in human SH-SY5Y neuroblastoma cells.
Neurodegenerative Diseases
Activity-Based Protein Profiling Delivers Selective Drug Candidate ABX-1431, a Monoacylglycerol Lipase Inhibitor, To Control Lipid Metabolism in Neurological Disorders.
Neurodegenerative Diseases
CB2 Receptors and Neuron-Glia Interactions Modulate Neurotoxicity Generated by MAGL Inhibition.
Neurodegenerative Diseases
Computationally driven discovery of phenyl(piperazin-1-yl)methanone derivatives as reversible monoacylglycerol lipase (MAGL) inhibitors.
Neurodegenerative Diseases
Design, Synthesis and Evaluation of 18F-labeled Monoacylglycerol Lipase Inhibitors as Novel Positron Emission Tomography Probes.
Neurodegenerative Diseases
Dysregulated expression of monoacylglycerol lipase is a marker for anti-diabetic drug metformin-targeted therapy to correct impaired neurogenesis and spatial memory in Alzheimer's disease.
Neuroinflammatory Diseases
2-Arachidonoylglycerol Reduces Proteoglycans and Enhances Remyelination in a Progressive Model of Demyelination.
Neuroinflammatory Diseases
A Novel Radiotracer for Imaging Monoacylglycerol Lipase in the Brain Using Positron Emission Tomography.
Neuroinflammatory Diseases
Deletion of Monoglyceride Lipase in Astrocytes Attenuates Lipopolysaccharide-induced Neuroinflammation.
Neuroinflammatory Diseases
Discovery of Trifluoromethyl Glycol Carbamates as Potent and Selective Covalent Monoacylglycerol Lipase (MAGL) Inhibitors for Treatment of Neuroinflammation.
Neuroinflammatory Diseases
Endocannabinoids: A Promising Impact for Traumatic Brain Injury.
Neuroinflammatory Diseases
Inhibition of monoacylglycerol lipase terminates diazepam-resistant status epilepticus in mice and its effects are potentiated by a ketogenic diet.
Neuroinflammatory Diseases
Monoacylglycerol lipase blockade impairs fine motor coordination and triggers cerebellar neuroinflammation through cyclooxygenase-2.
Neuroinflammatory Diseases
Monoacylglycerol lipase promotes Fc? receptor-mediated phagocytosis in microglia but does not regulate LPS-induced upregulation of inflammatory cytokines.
Non-alcoholic Fatty Liver Disease
The ménage à trois of autophagy, lipid droplets and liver disease.
Obesity
?/? Hydrolase Domain-containing 6 (ABHD6) Degrades the Late Endosomal/Lysosomal Lipid Bis(monoacylglycero)phosphate.
Obesity
Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer.
Obesity
Monoacylglycerol lipase deficiency affects diet-induced obesity, fat absorption, and feeding behavior in CB1 cannabinoid receptor-deficient mice.
Obesity
Over-Expression of Monoacylglycerol Lipase (MGL) in Small Intestine Alters Endocannabinoid Levels and Whole Body Energy Balance, Resulting in Obesity.
Osteoarthritis
Combatting joint pain and inflammation by dual inhibition of monoacylglycerol lipase and cyclooxygenase-2 in a rat model of osteoarthritis.
Osteoarthritis
Robust anti-nociceptive effects of MAG lipase inhibition in a model of osteoarthritis pain.
Osteolysis
JZL184, A Monoacylglycerol Lipase Inhibitor, Induces Bone Loss in a Multiple Myeloma Model of Immunocompetent Mice.
Osteosarcoma
JZL184, A Monoacylglycerol Lipase Inhibitor, Induces Bone Loss in a Multiple Myeloma Model of Immunocompetent Mice.
Parkinson Disease
Cannabinoid CB1 and CB2 Receptors, and Monoacylglycerol Lipase Gene Expression Alterations in the Basal Ganglia of Patients with Parkinson's Disease.
Parkinson Disease
Fatty acid amide hydrolase inhibition for the symptomatic relief of Parkinson's disease.
Peripheral Nervous System Diseases
Alterations in endocannabinoid tone following chemotherapy-induced peripheral neuropathy: effects of endocannabinoid deactivation inhibitors targeting fatty-acid amide hydrolase and monoacylglycerol lipase in comparison to reference analgesics following cisplatin treatment.
Prostatic Neoplasms
FABP5 coordinates lipid signaling that promotes prostate cancer metastasis.
Prostatic Neoplasms
JZL184, A Monoacylglycerol Lipase Inhibitor, Induces Bone Loss in a Multiple Myeloma Model of Immunocompetent Mice.
Prostatic Neoplasms
Monoacylglycerol Lipase Exerts Dual Control over Endocannabinoid and Fatty Acid Pathways to Support Prostate Cancer.
Prostatic Neoplasms
The influence of monoacylglycerol lipase inhibition upon the expression of epidermal growth factor receptor in human PC-3 prostate cancer cells.
Reperfusion Injury
Effects of monoacylglycerol lipase inhibitor URB602 on lung ischemia-reperfusion injury in mice.
Seizures
Equipotent Inhibition of Fatty Acid Amide Hydrolase and Monoacylglycerol Lipase - Dual Targets of the Endocannabinoid System to Protect against Seizure Pathology.
Seizures
Inhibition of monoacylglycerol lipase mediates a cannabinoid 1-receptor dependent delay of kindling progression in mice.
Seizures
Inhibition of monoacylglycerol lipase terminates diazepam-resistant status epilepticus in mice and its effects are potentiated by a ketogenic diet.
Sepsis
Endocannabinoid-mediated modulation of Gq protein-coupled receptor mediates vascular hyporeactivity to nor-adrenaline during polymicrobial sepsis.
Status Epilepticus
Inflammation and reactive oxygen species in status epilepticus: Biomarkers and implications for therapy.
Status Epilepticus
Inhibition of monoacylglycerol lipase terminates diazepam-resistant status epilepticus in mice and its effects are potentiated by a ketogenic diet.
Stroke
Monoacylglycerol Lipase Inhibitor is Safe when Combined with Delayed r-tPA Administration in Treatment of Stroke.
Stroke
Monoacylglycerol lipase inhibitor, JZL-184, confers neuroprotection in the mice middle cerebral artery occlusion model of stroke.
Tics
Monoacylglycerol Lipase Inhibition in Tourette Syndrome: A 12-Week, Randomized, Controlled Study.
Tourette Syndrome
Monoacylglycerol Lipase Inhibition in Tourette Syndrome: A 12-Week, Randomized, Controlled Study.
Tuberculosis
A monoacylglycerol lipase from Mycobacterium smegmatis Involved in bacterial cell interaction.
Tuberculosis
Characterization of an exported monoglyceride lipase from Mycobacterium tuberculosis possibly involved in the metabolism of host cell membrane lipids.
Tuberculosis
Enantioselective inhibition of microbial lipolytic enzymes by nonracemic monocyclic enolphosphonate analogues of cyclophostin.
Tuberculosis
Hemolytic phospholipase Rv0183 of Mycobacterium tuberculosis induces inflammatory response and apoptosis in alveolar macrophage RAW264.7 cells.
Tuberculosis
IL-6 release of Rv0183 antigen-stimulated whole blood is a potential biomarker for active tuberculosis patients.
Tuberculosis
Mycobacterium tuberculosis lipolytic enzymes as potential biomarkers for the diagnosis of active tuberculosis.
Tuberculosis
Potential Selective Inhibitors against Rv0183 of Mycobacterium tuberculosis Targeting Host Lipid Metabolism.
Tuberculosis
The crystal structure of monoacylglycerol lipase from M. tuberculosis reveals the basis for specific inhibition.
Whooping Cough
Lysophosphatidic acid (LPA) in malignant ascites stimulates motility of human pancreatic cancer cells through LPA1.
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0.02
1-decanoyl-rac-glycerol
at pH 7.4 and 37°C
0.0122
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol
at pH 7.4 and 37°C
0.0097 - 0.122
2-arachidonoylglycerol
0.084 - 0.162
4-Methylumbelliferyl butyrate
0.0088
arachidonoyl-7-hydroxy-6-methoxy-4-methylcoumarin ester
recombinant enzyme, in TME buffer, at 37°C
0.27
1(3)-monooleoylglycerol
-
-
0.01 - 0.016
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol
0.044
2-arachidonoylglycerol
-
pH and temperature not specified in the publication
0.2
4-nitrophenyl acetate
-
-
0.0098
7-hydroxycoumarinyl arachidonate
-
at pH 8 and 25°C, in 10% dimethyl sulfoxide
0.49
sn-2-monooleoylglycerol
-
-
additional information
additional information
-
0.0097
2-arachidonoylglycerol
at pH 7.4 and 37°C
0.012
2-arachidonoylglycerol
pH 7.4, 22°C, mutant H54A
0.0197
2-arachidonoylglycerol
recombinant enzyme, in TME buffer, at 37°C
0.022
2-arachidonoylglycerol
pH 7.4, 22°C, soluble wild-type variant
0.0222
2-arachidonoylglycerol
pH 7.4, 22°C, mutant H272A
0.0308
2-arachidonoylglycerol
pH 7.4, 22°C, mutant H272S
0.0362
2-arachidonoylglycerol
pH 7.4, 22°C, mutant H272Y
0.0366
2-arachidonoylglycerol
pH 7.4, 22°C, mutant H49A
0.122
2-arachidonoylglycerol
pH 7.4, 22°C, mutant H103A
0.084
4-Methylumbelliferyl butyrate
mutant enzyme L167Q/L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.084
4-Methylumbelliferyl butyrate
mutant enzyme L167Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.089
4-Methylumbelliferyl butyrate
mutant enzyme L171Q/L174Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.09
4-Methylumbelliferyl butyrate
mutant enzyme L169S/L176S/K160A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.105
4-Methylumbelliferyl butyrate
mutant enzyme L171Q, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.11
4-Methylumbelliferyl butyrate
mutant enzyme L169S/L176S/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.123
4-Methylumbelliferyl butyrate
mutant enzyme L169S/L176S/K36A/K226A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.124
4-Methylumbelliferyl butyrate
mutant enzyme L169S/L176S/K36A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.136
4-Methylumbelliferyl butyrate
mutant enzyme L169S/L176S, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.137
4-Methylumbelliferyl butyrate
mutant enzyme L169S/L176S/K165A, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.162
4-Methylumbelliferyl butyrate
wild type enzyme, in 20 mM PIPES, pH 7.0, and 150 mM NaCl at 37°C
0.01
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol
-
mutant enzyme C242A, at pH 7.4 and 37°C
0.013
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol
-
mutant enzyme C201A, at pH 7.4 and 37°C
0.015
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol
-
wild type enzyme, at pH 7.4 and 37°C
0.016
2-(15-deoxy-DELTA12,14-prostaglandin J2)-glycerol
-
mutant enzyme C208A, at pH 7.4 and 37°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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0.1
(3R)-1-(3,4-dimethylphenyl)-5-oxo-N-[(4-oxo-3,4-dihydrophthalazin-1-yl)methyl]pyrrolidine-3-carboxamide
Homo sapiens
IC50 around 0.1 mM, pH and temperature not specified in the publication
0.000039
(3R)-N-(3,5-dimethylphenyl)-1-[2-(5-fluoro-1H-indol-3-yl)ethyl]-5-oxopyrrolidine-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.1
(3S)-N-(1,3-benzodioxol-4-ylmethyl)-1-[4-[(2-chlorobenzyl)oxy]phenyl]-5-oxopyrrolidine-3-carboxamide
Homo sapiens
IC50 around 0.1 mM, pH and temperature not specified in the publication
0.0117
(4-(4-chlorobenzoyl)piperidin-1-yl)(4-methoxyphenyl)-methanone
Homo sapiens
pH 7.2, temperature not specified in the publication
0.2
12-deacetylsplendidin C
Homo sapiens
above, pH 7.2, temperature not specified in the publication
0.1139
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-(4-coumaroyl)-beta-D-glucopyranoside
Homo sapiens
pH 7.4, temperature not specified in the publication
0.088
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-2-O-acetyl-4-O-beta-D-glucopyranoside
Homo sapiens
pH 7.4, temperature not specified in the publication
0.1174
2-(4-hydroxyphenyl)ethyl alpha-L-rhamnopyranosyl-(1->3)-[alpha-L-rhamnopyranosyl-(1->6)]-beta-D-glucopyranoside
Homo sapiens
pH 7.4, temperature not specified in the publication
0.2
2-dehydroxysalvileucanthsin A
Homo sapiens
above, pH 7.2, temperature not specified in the publication
0.1
3-[(4S)-1-[2-(5-fluoro-1H-indol-3-yl)ethyl]-2,5-dioxoimidazolidin-4-yl]-N-[(1R,2R)-2-methylcyclohexyl]propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.000424
benzyl [4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)-2-methylphenyl]carbamate
Homo sapiens
pH and temperature not specified in the publication
0.0468
jewenol A
Homo sapiens
pH 7.2, temperature not specified in the publication
0.0002177
JZL184
Homo sapiens
pH 7.4, 22°C
0.0000054
methyl arachidonyl fluorophosphonate
Homo sapiens
pH 7.4, 22°C
5.38 - 6.64
N-arachidonylmaleimide
0.1
N-[3-(4-fluorophenyl)-6-oxopyrazolo[5,1-c]pyrido[4,3-e][1,2,4]triazin-7(6H)-yl]-2-(naphthalen-2-yloxy)acetamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.00001
N-[4-(1,3-benzothiazol-2-yl)phenyl]-2-(1H-benzotriazol-1-yl)acetamide
Homo sapiens
pH and temperature not specified in the publication
0.0032 - 0.0033
phenylmethylsulfonyl fluoride
0.2
pseudorosmaricin
Homo sapiens
above, pH 7.2, temperature not specified in the publication
0.0091
URB602
Homo sapiens
pH 7.4, 22°C
0.0000002
[4-[bis(1,3-benzodioxol-5-yl)methyl]-1-piperidinyl](1H-1,2,4-triazol-1-yl)methanone
Homo sapiens
at pH 7.4 and 37°C
0.00851
1-(hexa-5-enoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.0146
1-(hexa-5-enoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.133
1-(pent-4-enoyl)-(3R,4R)-3-[1(R)-(pent-4-enoyloxy)-ethyl]-4-(acetoxy)-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.00406
1-(pent-4-enoyl)-(3S)-3-[1(R)-(4-phenylbutanoyloxy)-ethyl]-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.00184
1-(pent-4-enoyl)-(3S)-3-[1(R)-(biphenylacetyloxy)-ethyl]-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.00472
1-(pent-4-enoyl)-(3S)-3-[1(R)-(hexa-5-enoyloxy)-ethyl]-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.0233
1-(pent-4-enoyl)-(3S)-3-[1(R)-(pent-4-enoyloxy)-ethyl]-azetidin-2-one
Homo sapiens
-
at 37°C for 10 min, in 10 mM Tris-HCl buffer, 1 mM EDTA, 0.1% (w/v) bovine serum albumin, pH 8.0
0.00021 - 0.0037
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)hydroxymethyl]piperidine-1-carboxylate
0.0031
AM404
Homo sapiens
-
pH and temperature not specified in the publication
0.0000009 - 0.0000017
AM6701
0.00184
arachidonoyltrifluoromethylketone
Homo sapiens
-
-
0.0049
CP55,940
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
Disulfiram
Homo sapiens
-
-
0.000076
methyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraen-1-ylphosphonofluoridate
Homo sapiens
-
-
0.000033 - 0.00016
methyl arachidonyl fluorophosphonate
0.00078
N-arachidonoyl dopamine
Homo sapiens
-
pH and temperature not specified in the publication
0.000155
N-arachidonyl maleimide
Homo sapiens
-
in 50 mM HEPES buffer, pH 8, 1 mM EDTA, and 10% dimethyl sulfoxide at 25°C for 60 min
0.0000091 - 0.0105
N-arachidonylmaleimide
0.005 - 0.02
N-benzoylthiocarbamic cyclohexylethyl ester
0.028
N-ethylmaleimide
Homo sapiens
-
-
0.00046
tetrahydrolipstatin
Homo sapiens
-
-
0.0011
troglitazone
Homo sapiens
-
pH and temperature not specified in the publication
0.0031
URB602
Homo sapiens
-
in 50 mM HEPES buffer, pH 8, 1 mM EDTA, and 10% dimethyl sulfoxide at 25°C for 60 min
0.00048 - 0.0011
[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3-yl)-2-methylphenyl]carbamic acid benzyl ester
additional information
additional information
Homo sapiens
-
-
-
5.38
N-arachidonylmaleimide
Homo sapiens
mutant C201A, at 37°C for 10 min, pH 8.0, in 50 mM Tris buffer
6.11
N-arachidonylmaleimide
Homo sapiens
mutant C242A, at 37°C for 10 min, pH 8.0, in 50 mM Tris buffer
6.27
N-arachidonylmaleimide
Homo sapiens
wild-type, at 37°C for 10 min, pH 8.0, in 50 mM Tris buffer
6.48
N-arachidonylmaleimide
Homo sapiens
mutant C208A/C242A, at 37°C for 10 min, pH 8.0, in 50 mM Tris buffer
6.64
N-arachidonylmaleimide
Homo sapiens
mutant C208A, at 37°C for 10 min, pH 8.0, in 50 mM Tris buffer
0.0032
phenylmethylsulfonyl fluoride
Homo sapiens
versus 7-4-nitrophenylacetate, pH 8.0-9.0, 37°C, recombinant enzyme
0.0033
phenylmethylsulfonyl fluoride
Homo sapiens
versus 7-hydroxycoumarinyl arachidonate, pH 8.0-9.0, 37°C, recombinant enzyme
0.00021
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)hydroxymethyl]piperidine-1-carboxylate
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, without Triton X-100
0.0017
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)hydroxymethyl]piperidine-1-carboxylate
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, in the presence of 0.2% (m/v) Triton X-100
0.0037
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)hydroxymethyl]piperidine-1-carboxylate
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, in the presence of 0.2% (m/v) Triton X-100
0.0000009
AM6701
Homo sapiens
-
native enzyme, in 50 mM Tris-HCl (pH 7.4) containing 8% DMSO, at room temperature
0.0000017
AM6701
Homo sapiens
-
recombinant enzyme, in 50 mM Tris-HCl (pH 7.4) containing 8% DMSO, at room temperature
0.0001
AM6702
Homo sapiens
-
native enzyme, in 50 mM Tris-HCl (pH 7.4) containing 8% DMSO, at room temperature
0.0028
AM6702
Homo sapiens
-
native enzyme, in 50 mM Tris-HCl (pH 7.4) containing 8% DMSO, at room temperature
0.0004
CAY10499
Homo sapiens
-
using 2-oleoylglycerol as a substrate
0.0005
CAY10499
Homo sapiens
-
using 4-nitophenyl acetate as a substrate
0.000033
methyl arachidonyl fluorophosphonate
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, without Triton X-100
0.000062
methyl arachidonyl fluorophosphonate
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, in the presence of 0.2% (m/v) Triton X-100
0.00016
methyl arachidonyl fluorophosphonate
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, in the presence of 0.2% (m/v) Triton X-100
0.0000091
N-arachidonylmaleimide
Homo sapiens
-
native enzyme, in 50 mM Tris-HCl (pH 7.4) containing 8% DMSO, at room temperature
0.0049
N-arachidonylmaleimide
Homo sapiens
-
using 2-oleoylglycerol as a substrate
0.0105
N-arachidonylmaleimide
Homo sapiens
-
using 4-nitophenyl acetate as a substrate
0.005
N-benzoylthiocarbamic cyclohexylethyl ester
Homo sapiens
-
using 4-nitophenyl acetate as a substrate
0.02
N-benzoylthiocarbamic cyclohexylethyl ester
Homo sapiens
-
using 2-oleoylglycerol as a substrate
0.00048
[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3-yl)-2-methylphenyl]carbamic acid benzyl ester
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, in the presence of 0.2% (m/v) Triton X-100
0.00061
[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3-yl)-2-methylphenyl]carbamic acid benzyl ester
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, without Triton X-100
0.0011
[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3-yl)-2-methylphenyl]carbamic acid benzyl ester
Homo sapiens
-
at 37°C, pH 7.0, incubation time of 15 min, in the presence of 0.2% (m/v) Triton X-100
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C201A
substantial decrease in the inhibitory potential
C201A/C208A/C242A
no significant inhibition by N-arachidonylmaleimide
C208A
increase in the inhibiting power of N-arachidonylmaleimide
C208A/C242A
increase in the inhibiting power of N-arachidonylmaleimide
C242A
very slight decrease in N-arachidonylmaleimide inhibitory potency
G111S
site-directed mutagenesis by overlap extension PCR, inactive mutant
G115S
site-directed mutagenesis by overlap extension PCR, inactive mutant
H103A
site-directed mutagenesis, the mutant shows 20fold reduced catalytic efficiency compared to wild-type
H269A
site-directed mutagenesis, structural comparison to the wild-type enzyme by NMR spectrometry
H272A
site-directed mutagenesis, the mutant shows 13fold reduced catalytic efficiency compared to wild-type
H272S
site-directed mutagenesis, the mutant shows 58fold reduced catalytic efficiency compared to wild-type
H272Y
site-directed mutagenesis, the muant shows 12fold reduced catalytic efficiency compared to wild-type
H49A
site-directed mutagenesis, the mutant shows 5fold reduced catalytic efficiency compared to wild-type
H54A
site-directed mutagenesis, structural comparison to the wild-type enzyme by NMR spectrometry, the mutant shows a dramatic 25000fold loss in hMGL catalytic efficiency compared to wild-type
L167Q/L171Q
the mutant shows increased catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L167Q/L174Q
the mutant shows increased catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L169S/L176S/K160A
the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L169S/L176S/K165A
the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L169S/L176S/K226A
the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L169S/L176S/K36A
the mutant shows about wild type catalytic efficiency with 4-methylumbelliferyl butyrate
L169S/L176S/K36A/K226A
the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L171Q
the mutant shows about wild type catalytic efficiency with 4-methylumbelliferyl butyrate
L171Q/L174Q
the mutant shows increased catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
S113A
site-directed mutagenesis by overlap extension PCR, inactive mutant
S122C
site-directed mutagenesis, structural comparison to the wild-type enzyme by NMR spectrometry
C201A
-
the mutation causes a significant reduction in overall activity particularly skewing the balanced hydrolysis of monoacyl glycerol isomers to favor the 2-isomer over the 1-isomer
C215A
-
the mutation does not affect MGL hydrolytic activity and displays heightened N-arachidonylmaleimide sensitivity
C215A/C249A
-
the mutation does not affect MGL hydrolytic activity
C249A
-
the mutation does not affect MGL hydrolytic activity and displays reduced N-arachidonylmaleimide sensitivity
D239T
-
the mutation substantially compromises enzyme activity
Y194A
-
the mutation causes a significant reduction in overall activity
Y194A/C242A
-
the mutation causes a significant reduction in overall activity
L169S/L176S
the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate and increased catalytic efficiency with umbelliferyl arachidonate compared to the wild type enzyme
L169S/L176S
the mutant shows reduced catalytic efficiency with 4-methylumbelliferyl butyrate compared to the wild type enzyme
L169S/L176S
site-directed mutagenesis, hMGL function is not significantly compromised by the mutation, structural comparison to the wild-type enzyme by NMR spectrometry
C208A
-
the mutation does not affect enzyme catalytic activity
C208A
-
the mutation causes a significant reduction in overall activity particularly skewing the balanced hydrolysis of monoacyl glycerol isomers to favor the 2-isomer over the 1-isomer
C242A
-
the mutation does not affect enzyme catalytic activity
C242A
-
the mutation causes a significant reduction in overall activity particularly skewing the balanced hydrolysis of monoacyl glycerol isomers to favor the 2-isomer over the 1-isomer
additional information
computational modeling shows that amino acid changes of the GxSxG motif in AtMAGL6 alters the nucleophilic elbow structure, which is the active site of MAGLs. Mutating the GxSxG motif in the recombinant maltose binding protein (MBP):AtMAGL6 protein to SxSxG, GxAxG, and GxSxS motifs completely demolishes the activities of the mutant MAGL
additional information
the transgene of human MGLL in macrophages largely prolonges the survival of MC-38 tumor-bearing mice
additional information
-
the transgene of human MGLL in macrophages largely prolonges the survival of MC-38 tumor-bearing mice
additional information
-
construction of a HeLa cell line, HeLa-MGLi, with stable repression of enzyme expression by RNAi silencing, the cells show 20% of wild-type cell line enzyme activity
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Somma-Delpero, C.; Valette, A.; Lepetit-Thevenin, J.; Nobili, O.; Boyer, J.; Verine, A.
Purification and properties of a monoacylglycerol lipase in human erythrocytes
Biochem. J.
312
519-525
1995
Homo sapiens
brenda
Dinh, T.P.; Kathuria, S.; Piomelli, D.
RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol
Mol. Pharmacol.
66
1260-1264
2004
Homo sapiens, Rattus norvegicus
brenda
Labar, G.; Bauvois, C.; Muccioli, G.G.; Wouters, J.; Lambert, D.M.
Disulfiram is an inhibitor of human purified monoacylglycerol lipase, the enzyme regulating 2-arachidonoylglycerol signaling
Chembiochem
8
1293-1297
2007
Homo sapiens
brenda
Chon, S.H.; Zhou, Y.X.; Dixon, J.L.; Storch, J.
Intestinal monoacylglycerol metabolism: developmental and nutritional regulation of monoacylglycerol lipase and monoacylglycerol acyltransferase
J. Biol. Chem.
282
33346-33357
2007
Homo sapiens, Mus musculus, Mus musculus C57BL/6
brenda
Saario, S.M.; Poso, A.; Juvonen, R.O.; Jaervinen, T.; Salo-Ahen, O.M.
Fatty acid amide hydrolase inhibitors from virtual screening of the endocannabinoid system
J. Med. Chem.
49
4650-4656
2006
Homo sapiens, Rattus norvegicus
brenda
Zvonok, N.; Pandarinathan, L.; Williams, J.; Johnston, M.; Karageorgos, I.; Janero, D.R.; Krishnan, S.C.; Makriyannis, A.
Covalent inhibitors of human monoacylglycerol lipase: ligand-assisted characterization of the catalytic site by mass spectrometry and mutational analysis
Chem. Biol.
15
854-862
2008
Homo sapiens
brenda
Muccioli, G.G.; Labar, G.; Lambert, D.M.
CAY10499, a novel monoglyceride lipase inhibitor evidenced by an expeditious MGL assay
ChemBioChem
9
2704-2710
2008
Homo sapiens
brenda
Zvonok, N.; Williams, J.; Johnston, M.; Pandarinathan, L.; Janero, D.R.; Li, J.; Krishnan, S.C.; Makriyannis, A.
Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification
J. Proteome Res.
7
2158-2164
2008
Rattus norvegicus (Q8R431), Homo sapiens (Q99685), Homo sapiens
brenda
Holtfrerich, A.; Makharadze, T.; Lehr, M.
High-performance liquid chromatography assay with fluorescence detection for the evaluation of inhibitors against human recombinant monoacylglycerol lipase
Anal. Biochem.
399
218-224
2010
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Wang, Y.; Chanda, P.; Jones, P.G.; Kennedy, J.D.
A fluorescence-based assay for monoacylglycerol lipase compatible with inhibitor screening
Assay Drug Dev. Technol.
6
387-393
2008
Homo sapiens
brenda
Labar, G.; Bauvois, C.; Borel, F.; Ferrer, J.L.; Wouters, J.; Lambert, D.M.
Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
ChemBioChem
11
218-227
2010
Homo sapiens (Q99685), Homo sapiens
brenda
Vandevoorde, S.
Overview of the chemical families of fatty acid amide hydrolase and monoacylglycerol lipase inhibitors
Curr. Top. Med. Chem.
8
247-267
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Bowman, A.L.; Makriyannis, A.
Refined homology model of monoacylglycerol lipase: toward a selective inhibitor
J. Comput. Aided Mol. Des.
23
799-806
2009
Homo sapiens (Q99685)
brenda
Feledziak, M.; Michaux, C.; Urbach, A.; Labar, G.; Muccioli, G.G.; Lambert, D.M.; Marchand-Brynaert, J.
beta-Lactams derived from a carbapenem chiron are selective inhibitors of human fatty acid amide hydrolase versus human monoacylglycerol lipase
J. Med. Chem.
52
7054-7068
2009
Homo sapiens
brenda
Bjoerklund, E.; Noren, E.; Nilsson, J.; Fowler, C.J.
Inhibition of monoacylglycerol lipase by troglitazone, N-arachidonoyl dopamine and the irreversible inhibitor JZL184: comparison of two different assays
Br. J. Pharmacol.
161
1512-1526
2010
Homo sapiens, Rattus norvegicus
brenda
Nomura, D.K.; Long, J.Z.; Niessen, S.; Hoover, H.S.; Ng, S.W.; Cravatt, B.F.
Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
Cell
140
49-61
2010
Homo sapiens
brenda
Bertrand, T.; Auge, F.; Houtmann, J.; Rak, A.; Vallee, F.; Mikol, V.; Berne, P.; Michot, N.; Cheuret, D.; Hoornaert, C.; Mathieu, M.
Structural basis for human monoglyceride lipase inhibition
J. Mol. Biol.
396
663-673
2010
Homo sapiens
brenda
Karageorgos, I.; Tyukhtenko, S.; Zvonok, N.; Janero, D.R.; Sallum, C.; Makriyannis, A.
Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism
Mol. Biosyst.
6
1381-1388
2010
Homo sapiens
brenda
Schalk-Hihi, C.; Schubert, C.; Alexander, R.; Bayoumy, S.; Clemente, J.C.; Deckman, I.; DesJarlais, R.L.; Dzordzorme, K.C.; Flores, C.M.; Grasberger, B.; Kranz, J.K.; Lewandowski, F.; Liu, L.; Ma, H.; Maguire, D.; Macielag, M.J.; McDonnell, M.E.; Mezzasalma Haarlander, T.; Miller, R.; Milligan, C.; R, R.e.
Crystal structure of a soluble form of human monoglyceride lipase in complex with an inhibitor at 1.35 A resolution
Protein Sci.
20
670-683
2011
Homo sapiens (Q99685), Homo sapiens
brenda
Karageorgos, I.; Wales, T.E.; Janero, D.R.; Zvonok, N.; Vemuri, V.K.; Engen, J.R.; Makriyannis, A.
Active-site inhibitors modulate the dynamic properties of human monoacylglycerol lipase: a hydrogen exchange mass spectrometry study
Biochemistry
52
5016-5026
2013
Homo sapiens
brenda
Afzal, O.; Kumar, S.; Kumar, R.; Firoz, A.; Jaggi, M.; Bawa, S.
Docking based virtual screening and molecular dynamics study to identify potential monoacylglycerol lipase inhibitors
Bioorg. Med. Chem. Lett.
24
3986-3996
2014
Homo sapiens (Q99685), Homo sapiens
brenda
Li, C.; Vilches-Flores, A.; Zhao, M.; Amiel, S.A.; Jones, P.M.; Persaud, S.J.
Expression and function of monoacylglycerol lipase in mouse beta-cells and human islets of Langerhans
Cell. Physiol. Biochem.
30
347-358
2012
Homo sapiens, Mus musculus
brenda
Laitinen, T.; Navia-Paldanius, D.; Rytilahti, R.; Marjamaa, J.J.; Ka?izkova, J.; Parkkari, T.; Pantsar, T.; Poso, A.; Laitinen, J.T.; Savinainen, J.R.
Mutation of Cys242 of human monoacylglycerol lipase disrupts balanced hydrolysis of 1- and 2-monoacylglycerols and selectively impairs inhibitor potency
Mol. Pharmacol.
85
510-519
2014
Homo sapiens
brenda
Savinainen, J.R.; Kansanen, E.; Pantsar, T.; Navia-Paldanius, D.; Parkkari, T.; Lehtonen, M.; Laitinen, T.; Nevalainen, T.; Poso, A.; Levonen, A.L.; Laitinen, J.T.
Robust hydrolysis of prostaglandin glycerol esters by human monoacylglycerol lipase (MAGL)
Mol. Pharmacol.
86
522-535
2014
Homo sapiens (Q99685), Homo sapiens
brenda
Chen, H.; Tian, R.; Ni, Z.; Zhang, Z.; Chen, H.; Guo, Q.; Saier, M.H.
Conformational transition pathway in the inhibitor binding process of human monoacylglycerol lipase
Protein J.
33
503-511
2014
Homo sapiens
brenda
Lauria, S.; Casati, S.; Ciuffreda, P.
Synthesis and characterization of a new fluorogenic substrate for monoacylglycerol lipase and application to inhibition studies
Anal. Bioanal. Chem.
407
8163-8167
2015
Homo sapiens (Q99685), Homo sapiens
brenda
Kim, R.; Suh, M.
The GxSxG motif of Arabidopsis monoacylglycerol lipase (MAGL6 and MAGL8) is essential for their enzyme activities
Appl. Biol. Chem.
59
833-840
2016
Arabidopsis thaliana (O49284), Arabidopsis thaliana (O80959), Arabidopsis thaliana (Q8H133), Homo sapiens (Q99685)
-
brenda
De Leo, M.; Huallpa, C.G.; Alvarado, B.; Granchi, C.; Poli, G.; De Tommasi, N.; Braca, A.
New diterpenes from Salvia pseudorosmarinus and their activity as inhibitors of monoacylglycerol lipase (MAGL)
Fitoterapia
130
251-258
2018
Homo sapiens (Q99685)
brenda
Tyukhtenko, S.; Karageorgos, I.; Rajarshi, G.; Zvonok, N.; Pavlopoulos, S.; Janero, D.R.; Makriyannis, A.
Specific inter-residue interactions as determinants of human monoacylglycerol lipase catalytic competency a role for global conformational chanages
J. Biol. Chem.
291
2556-2565
2016
Homo sapiens (Q99685), Homo sapiens
brenda
Xiang, W.; Shi, R.; Kang, X.; Zhang, X.; Chen, P.; Zhang, L.; Hou, A.; Wang, R.; Zhao, Y.; Zhao, K.; Liu, Y.; Ma, Y.; Luo, H.; Shang, S.; Zhang, J.; He, F.; Yu, S.; Gan, L.; Shi, C.; Li, Y.; Yang, W.; Liang, H.; Miao, H.
Monoacylglycerol lipase regulates cannabinoid receptor 2-dependent macrophage activation and cancer progression
Nat. Commun.
9
2574
2018
Mus musculus (O35678), Homo sapiens (Q99685), Homo sapiens
brenda
Beladjila, K.A.; Berrehal, D.; De Tommasi, N.; Granchi, C.; Bononi, G.; Braca, A.; De Leo, M.
New phenylethanoid glycosides from Cistanche phelypaea and their activity as inhibitors of monoacylglycerol lipase (MAGL)
Planta Med.
84
710-715
2018
Homo sapiens (Q99685)
brenda