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Information on EC 3.1.1.23 - acylglycerol lipase and Organism(s) Rattus norvegicus and UniProt Accession Q8R431
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3.1.1.23 acylglycerol lipaseSpecify your search results
Word Map
- 3.1.1.23
-
endocannabinoids
- cannabinoids
- 2-arachidonoylglycerol
- amide
- anandamide
- agonist
- diacylglycerol
- pain
-
arachidonic
- synaptic
- phospholipase
-
2-arachidonoyl
-
lipolytic
- adipose
- lipases
- prostaglandin
- triacylglycerols
-
anxiety
-
activity-based
-
presynaptic
-
rimonabant
-
nociceptive
-
analgesia
-
antinociceptive
- cannabis
-
cannabimimetic
-
neuropathic
- n-arachidonoylethanolamine
-
hormone-sensitive
- tetrahydrolipstatin
- 4-nitrophenyl
- n-acylethanolamine
- fluorophosphonate
- diagnostics
- hyperalgesia
- allodynia
-
endocannabinoid-mediated
- drug development
- nape-pld
-
depolarization-induced
- medicine
- chlorpyrifos
- synthesis
-
psychoactive
- delta9-tetrahydrocannabinol
-
catalepsy
- pharmacology
- lysophospholipase
- 2-monoacylglycerols
- marijuana
- oleoylethanolamide
-
post-heparin
-
anxiety-like
- palmitoylethanolamide
-
anxiolytic
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
monoacylglycerol lipase, monoglyceride lipase, mag lipase, rv0183, monoacylglycerol hydrolase, monoglyceride hydrolase, yju3p, mag hydrolase, acylglycerol lipase, msmeg_0220, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fatty acyl monoester lipase
-
-
-
-
monoacylglycerol hydrolase
-
-
-
-
monoacylglycerol lipase
monoglyceridase
-
-
-
-
monoglyceride hydrolase
-
-
-
-
monoglyceride lipase
monoglyceridyllipase
-
-
-
-
monoacylglycerol lipase
-
-
-
-
monoacylglycerol lipase
-
-
monoglyceride lipase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycerol-ester acylhydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9040-75-9
-
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
1,3-dihydroxypropan-2-yl 4-pyren-1-ylbutanoate
pyrenylbutanoic acid + glycerol
-
-
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
-
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
the enzyme is responsible for degradation of 2-arachidonoylglycerol in the brain
-
-
?
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
presynaptic MGL not only hydrolyzes 2-arachidonoylglycerol released from activated postsynaptic neurons but also contributes to degradation of constitutively produced 2-arachidonoylglycerol and prevention of its accumulation around presynaptic terminals. Thus, the MGL activity determines basal endocannabinoid tone and terminates retrograde endocannabinoid signaling in the hippocampus
-
-
?
2-oleoylglycerol + H2O
oleic acid + glycerol
-
-
-
-
?
2-oleoylglycerol + H2O
oleic acid + glycerol
-
Cys208 plays an important role in MGL function
-
-
?
additional information
?
-
enzyme does not hydrolyze palmitoylethanolamine, enzyme preferentially hydrolyzes 2-monoglycerides
-
?
additional information
?
-
-
no activity against long-chain diacylglycerols and triacylglycerols, cholesterol ester, or lysophosphatidylcholine
-
-
?
additional information
?
-
-
enzyme exhibits both phosphatidic acid-preferring phospholipase A2 and monoacylglycerol lipase activities with a modest specificity towards unsaturated acyl chains, veryl low di- and triaclyglycerol lipase activity
-
?
additional information
?
-
-
monoacylglycerol lipase is required in the final hydrolysis of 2-monoacylglycerols produced by hormone-sensitive lipase
-
-
?
additional information
?
-
-
the enzyme is involved in prostaglandin metabolism in brain particulate fractions
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
-
-
?
2-arachidonoylglycerol + H2O
glycerol + arachidonic acid
-
presynaptic MGL not only hydrolyzes 2-arachidonoylglycerol released from activated postsynaptic neurons but also contributes to degradation of constitutively produced 2-arachidonoylglycerol and prevention of its accumulation around presynaptic terminals. Thus, the MGL activity determines basal endocannabinoid tone and terminates retrograde endocannabinoid signaling in the hippocampus
-
-
?
2-arachidonoylglycerol + H2O
arachidonic acid + glycerol
-
the enzyme is responsible for degradation of 2-arachidonoylglycerol in the brain
-
-
?
additional information
?
-
-
monoacylglycerol lipase is required in the final hydrolysis of 2-monoacylglycerols produced by hormone-sensitive lipase
-
-
?
additional information
?
-
-
the enzyme is involved in prostaglandin metabolism in brain particulate fractions
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
JZL184
significantly decreases lipolysis and increases both mono- and diacyglycerol species in INS-1 cells. Analysis of the kinetics of glucose-stimulated insulin secretion (GSIS) shows that inhibition is greater during the sustained phase of secretion. JZL184 does not significantly affect basal insulin secretion at any concentration tested. Kinetics, overview
MJN110
inhibits glucose-stimulated insulin secretion and depolarization-induced insulin secretion in INS-1 (832/13) cells
URB602
inhibits glucose-stimulated insulin secretion and depolarization-induced insulin secretion in INS-1 (832/13) cells
(2S)-6-[4-(hexyloxy)phenyl]hexane-1,2-diamine
-
exhibits weak inhibitory activity (25.9%)
(2S,9Z)-octadec-9-ene-1,2-diamine
-
selectively inhibits MGL by 49.9%. The presence of a long monounsaturated chain corresponding to oleic acid is a key requirement for the selective inhibition of MGL
(4-amidinophenyl) methanesulfonyl fluoride
-
i.e. APMSF, inhibits at 0.5 mM
(5E)-5-(3-methylbutylidene)-2-thioxo-1,3-thiazolidin-4-one
-
weak inhibitory effect
(5Z,8Z,11Z,14Z)-eicosantetraenoic acid 3-thienyl methyl ester
-
i.e. CAY-10402, 14% inhibition at 0.1 mM
1-(20-cyano-16,16-dimethyl-eicosa-5,8,11,14-tetraenoyl)glycerol
-
i.e. O-223
1-(20-hydroxy-16,16-dimethyl-eicosa-5,8,11,14-tetraenoyl)glycerol
-
i.e. O-224
1-arachidin
-
11% inhibition of the membraneous enzyme at 0.1 mM, 19% inhibition of the cytosolic enzyme at 0.1 mM
1-myristin
-
IC50 value for the membraneous and the cytosolic enzyme is 0.032 mM, complete inhibition is possible
1-nor-arachidonoyl-3-(2'3-dihydroxypropyl) urea
-
i.e. O-1502, 39% inhibition at 0.1 mM
1-palmitin
-
44% inhibition of the membraneous enzyme at 0.1 mM, 38% inhibition of the cytosolic enzyme at 0.1 mM
2,3-dihydroxypropyl (11Z)-icos-11-enoate
-
i.e. O-4066, IC50 value for the membraneous enzyme is 0.026 mM, for the cytosolic enzyme 0.019 mM, complete inhibition of the membraneous enzyme is possible, maximal inhibition of the cytosolic enzyme of 79%
2,3-dihydroxypropyl (11Z,14Z)-icosa-11,14-dienoate
-
i.e. O-3907, IC50 value for the membraneous enzyme is 0.016 mM, for the cytosolic enzyme 0.0051 mM, complete inhibition is possible
2,3-dihydroxypropyl (4Z,7Z,10Z,13Z)-17-ethylcycloheptadeca-4,7,10,13-tetraene-1-carboxylate
-
i.e. O-1428, IC50 value for the membraneous enzyme is 0.071 mM, for the cytosolic enzyme 0.015 mM, complete inhibition is possible
2,3-dihydroxypropyl (5Z)-icos-5-enoate
-
i.e. 3908, IC50 value for the membraneous enzyme is 0.056 mM, for the cytosolic enzyme 0.021 mM, complete inhibition of the membraneous enzyme is possible, maximal inhibition of the cytosolic enzyme of 65%
2,3-dihydroxypropyl (5Z,8Z,11Z)-2-ethylcycloheptadeca-5,8,11-triene-1-carboxylate
-
i.e. O-3973, IC50 value for the membraneous enzyme is 0.0083 mM, for the cytosolic enzyme 0.0042 mM, complete inhibition is possible
2,3-dihydroxypropyl (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate
-
i.e. O-3832, IC50 value for the membraneous enzyme is 0.017 mM, for the cytosolic enzyme 0.0082 mM, complete inhibition is possible
2,3-dihydroxypropyl (6Z,9Z,12Z,15Z)-cyclohenicosa-6,9,12,15-tetraene-1-carboxylate
-
IC50 value for the membraneous enzyme is 0.0051 mM, for the cytosolic enzyme 0.0058 mM, complete inhibition is possible
2,3-dihydroxypropyl (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoate
-
IC50 value for the membraneous enzyme is 0.011 mM, for the cytosolic enzyme 0.0045 mM, complete inhibition is possible
2,3-dihydroxypropyl (8Z,11Z,14Z)-icosa-8,11,14-trienoate
-
i.e. 3846, IC50 value for the membraneous enzyme is 0.073 mM, for the cytosolic enzyme 0.0075 mM, complete inhibition is possible
2-arachidonoylglycerol
-
inhibits the hydrolysis of cytosolic 2-oleoylglycerol, IC50 value is 0.013 mM, the affinity for the enzyme is highest with an arachidonyl side chain and decreases to fatty acids of shorter chain length
4-nitrophenyl 4-[bis(1,3-benzodioxol-5-yl)hydroxymethyl]piperidine-1-carboxylate
-
JZL184
6-methyl-2-[(4-methylphenyl)amino]-4H-3,1-benzoxazin-4-one
-
URB754, inhibition of brain MAGL expressed in HeLa cells, no inhibition of membrane-bound MAGL. Is not selective for MAGL
alpha-methyl-1-arachidonoyl glycerol
-
compound O-1428, inhibits both cytosolic and membrane-bound MAGL
arachidonoyltrifluoromethyl ketone
-
i.e. ATFMK, inhibition is reversible by AM281
dihydrocelastrol
-
inhibits MGL activity, albeit less potently than pristimerin
dihydrocelastryl diacetate
-
inhibits MGL activity, albeit less potently than pristimerin
euphol
-
inhibits MGL activity with high potency. Blocks MGL activity through a reversible and noncompetitive mechanism, which is apparently identical to that of pristimerin
N-(2-hydroxyethyl)-2-oxopentadecanamide
-
exhibits weak inhibitory activity (27.5%) and no selectivity towards MGL
N-(4-hydroxy-2-methylphenyl)arachidonylamide
-
i.e. VDM11, an anandamide uptake inhibitor, substrate of fatty acid amide hydrolase, EC 3.5.1.4, IC50 is 0.021 mM
N-(4-hydroxyphenyl)arachidonylamide
-
i.e. AM404, an anandamide uptake inhibitor, substrate of fatty acid amide hydrolase, EC 3.5.1.4, IC50 is 0.020 mM
pristimerin
-
inhibits MGL activity with high potency. Addition to purified MGL produces an almost immediate blockade of MGL activity. Inhibits MGL through a mechanism that is rapid, reversible, and noncompetitive
[1,1'-biphenyl]-3-yl-carbamic acid, cyclohexyl ester
-
URB602, noncompetetive selective inhibitor
[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3-yl)-2-methylphenyl]carbamic acid benzyl ester
-
CAY10499
1-arachidonoylglycerol
-
IC50 value for the membraneous enzyme is 0.0095 mM, for the cytosolic enzyme 0.0071 mM, complete inhibition is possible
1-arachidonoylglycerol
-
inhibits the hydrolysis of cytosolic 2-oleoylglycerol, IC50 value is 0.017 mM, the affinity for the enzyme is highest with an arachidonyl side chain and decreases to fatty acids of shorter chain length
2-octyl-4-isothiazolin-3-one
-
octhilinone, inhibits purified recombinant MGL through a partially reversible mechanism that involves a specific interaction with cysteine 208
arachidonoyl trifluoromethylketone
-
the affinity for the enzyme is highest with an arachidonyl side chain and decreases to fatty acids of shorter chain length
arachidonoyl trifluoromethylketone
-
causes a gradual suppression of cannabinoid-sensitive IPSCs in cultured hippocampal neurons, the suppression is reversed by blocking CB1 receptors and is attenuated by inhibiting 2-AG synthesis, overview
methyl arachidonyl fluorophosphonate
-
causes a gradual suppression of cannabinoid-sensitive IPSCs in cultured hippocampal neurons, the suppression is reversed by blocking CB1 receptors and is attenuated by inhibiting 2-AG synthesis, overview
N-arachidonylmaleimide
-
inhibitory effect is attributed to the ability of this compound to react with C242 and form a Michael addition product
additional information
inhibition by bulky maleimides derivatives is due to steric hindrance of substrate binding after alkylation of cysteines 242 and/or 208, no inhibition by succimide and N-arachidonylsuccimide
-
additional information
-
immunodepletion of the recombinant enzyme leads to 50% reduced activity
-
additional information
-
inhibitory potency of different 1-arachidonic acid analogues, the chain length of the fatty acid is important for affinity and inhibition, while methylations of the fatty acids do not influence the inhibitory potency, overview
-
additional information
-
no inhibition by URB597, bovine serum albumin decreases the inhibitory effect of arachidonoyl-based compounds, e.g. VDM11
-
additional information
-
inhibitors of other endocannabinoid hydrolyzing enzymes, fatty acid amide hydrolase and cyclooxygenase-2, have no effect on the 2-AG-induced IPSC suppression
-
additional information
-
3-methoxy-N-phenyl-1,2,4-thiadiazol-5-amine and 3-propoxy-2-benzofuran-1(3H)-one do not inhibit
-
additional information
-
(2S)-6-phenylhexane-1,2-diamine and (2S,9Z)-2-aminooctadec-9-enamide show no inhibition
-
additional information
-
is not inhibited by 1 mM N-arachidonylsuccinimide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000014
2-oleoylglycerol
-
in the presence of 0.0005 mM pristimerin, at pH 7.5, 37°C
0.000024
2-oleoylglycerol
-
in the presence of 0.0003 mM pristimerin, at pH 7.5, 37°C
0.000027
2-oleoylglycerol
-
in the presence of 0.0001 mM pristimerin, at pH 7.5, 37°C
0.000028
2-oleoylglycerol
-
in the presence of vehicle (0.1% DMSO), at pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(5E)-5-(3-methylbutylidene)-2-thioxo-1,3-thiazolidin-4-one
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.032
1-myristin
Rattus norvegicus
-
IC50 value for the membraneous and the cytosolic enzyme is 0.032 mM, complete inhibition is possible
0.026
2,3-dihydroxypropyl (11Z)-icos-11-enoate
Rattus norvegicus
-
i.e. O-4066, IC50 value for the membraneous enzyme is 0.026 mM, for the cytosolic enzyme 0.019 mM, complete inhibition of the membraneous enzyme is possible, maximal inhibition of the cytosolic enzyme of 79%
0.016
2,3-dihydroxypropyl (11Z,14Z)-icosa-11,14-dienoate
Rattus norvegicus
-
i.e. O-3907, IC50 value for the membraneous enzyme is 0.016 mM, for the cytosolic enzyme 0.0051 mM, complete inhibition is possible
0.071
2,3-dihydroxypropyl (4Z,7Z,10Z,13Z)-17-ethylcycloheptadeca-4,7,10,13-tetraene-1-carboxylate
Rattus norvegicus
-
i.e. O-1428, IC50 value for the membraneous enzyme is 0.071 mM, for the cytosolic enzyme 0.015 mM, complete inhibition is possible
0.056
2,3-dihydroxypropyl (5Z)-icos-5-enoate
Rattus norvegicus
-
i.e. 3908, IC50 value for the membraneous enzyme is 0.056 mM, for the cytosolic enzyme 0.021 mM, complete inhibition of the membraneous enzyme is possible, maximal inhibition of the cytosolic enzyme of 65%
0.0083
2,3-dihydroxypropyl (5Z,8Z,11Z)-2-ethylcycloheptadeca-5,8,11-triene-1-carboxylate
Rattus norvegicus
-
i.e. O-3973, IC50 value for the membraneous enzyme is 0.0083 mM, for the cytosolic enzyme 0.0042 mM, complete inhibition is possible
0.017
2,3-dihydroxypropyl (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate
Rattus norvegicus
-
i.e. O-3832, IC50 value for the membraneous enzyme is 0.017 mM, for the cytosolic enzyme 0.0082 mM, complete inhibition is possible
0.0051
2,3-dihydroxypropyl (6Z,9Z,12Z,15Z)-cyclohenicosa-6,9,12,15-tetraene-1-carboxylate
Rattus norvegicus
-
IC50 value for the membraneous enzyme is 0.0051 mM, for the cytosolic enzyme 0.0058 mM, complete inhibition is possible
0.011
2,3-dihydroxypropyl (7Z,10Z,13Z,16Z)-docosa-7,10,13,16-tetraenoate
Rattus norvegicus
-
IC50 value for the membraneous enzyme is 0.011 mM, for the cytosolic enzyme 0.0045 mM, complete inhibition is possible
0.073
2,3-dihydroxypropyl (8Z,11Z,14Z)-icosa-8,11,14-trienoate
Rattus norvegicus
-
i.e. 3846, IC50 value for the membraneous enzyme is 0.073 mM, for the cytosolic enzyme 0.0075 mM, complete inhibition is possible
0.013
2-arachidonoylglycerol
Rattus norvegicus
-
inhibits the hydrolysis of cytosolic 2-oleoylglycerol, IC50 value is 0.013 mM, the affinity for the enzyme is highest with an arachidonyl side chain and decreases to fatty acids of shorter chain length
0.000239
2-methyl-4-isothiazolin-3-one
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.000059
2-octyl-benzo[d]isothiazol-3-one
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.000043
2-oleoyl-4-isothiazolin-3-one
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.028
3-methoxy-N-phenyl-1,2,4-thiadiazol-5-amine
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.0002
6-methyl-2-[(4-methylphenyl)amino]-4H-3,1-benzoxazin-4-one
Rattus norvegicus
-
MAGL expressed in HeLa cells
0.021
N-(4-hydroxy-2-methylphenyl)arachidonylamide
Rattus norvegicus
-
i.e. VDM11, an anandamide uptake inhibitor, substrate of fatty acid amide hydrolase, EC 3.5.1.4, IC50 is 0.021 mM
0.02
N-(4-hydroxyphenyl)arachidonylamide
Rattus norvegicus
-
i.e. AM404, an anandamide uptake inhibitor, substrate of fatty acid amide hydrolase, EC 3.5.1.4, IC50 is 0.020 mM
0.0027
N-ethylmaleimide
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.0095
1-arachidonoylglycerol
Rattus norvegicus
-
IC50 value for the membraneous enzyme is 0.0095 mM, for the cytosolic enzyme 0.0071 mM, complete inhibition is possible
0.017
1-arachidonoylglycerol
Rattus norvegicus
-
inhibits the hydrolysis of cytosolic 2-oleoylglycerol, IC50 value is 0.017 mM, the affinity for the enzyme is highest with an arachidonyl side chain and decreases to fatty acids of shorter chain length
0.000151
2-octyl-4-isothiazolin-3-one
Rattus norvegicus
-
wild-type, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.000722
2-octyl-4-isothiazolin-3-one
Rattus norvegicus
-
mutant C208G, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.00003
N-arachidonylmaleimide
Rattus norvegicus
-
wild-type, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.000046
N-arachidonylmaleimide
Rattus norvegicus
-
recombinant purified enzyme, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/mlL bovine serum albumin, fatty acid-free
0.000107
N-arachidonylmaleimide
Rattus norvegicus
-
mutant C242G, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.000442
N-arachidonylmaleimide
Rattus norvegicus
-
mutant C201G, for 10 min at 37°C, in 50 mM Tris-HCl, pH 8.0, 0.5 mg/ml bovine serum albumin, fatty acid-free
0.028
[1,1'-biphenyl]-3-yl-carbamic acid, cyclohexyl ester
Rattus norvegicus
-
cytosolic MAGL
0.075
[1,1'-biphenyl]-3-yl-carbamic acid, cyclohexyl ester
Rattus norvegicus
-
MAGL expressed in HeLa cells
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.5
-
pH 5.0: about 55% of maximal activity, pH 9.5: about 85% of maximal activity, enzyme from cytosol
6 - 9.5
-
pH 6.0: about 45% of maximal activity, pH 9.5: about 65% of maximal activity, enzyme from plasma membrane
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expressed in nerve cell bodies and nerve fibres of the enteric nervous system
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
inhibition of monoacylglycerol lipase activity decreases glucose-stimulated insulin secretion in INS-1 (832/13) cells and rat islets
physiological function
monoacylglycerol lipase (MGL) activity catalyzes the final step in triacylglycerol breakdown, namely the hydrolysis of monoacylglycerol to glycerol and free fatty acid. The final common step in the triggering pathway of glucose-stimulated insulin secretion (GSIS) and depolarization is a rise in cytosolic Ca2+, which directly promotes the fusion of insulin granules with the plasma membrane. The ability of JZL184 to inhibit both GSIS and KCl/DZ induced insulin secretion implied a strong likelihood that Ca2+ is reduced in response to these stimuli
malfunction
-
MGL inhibitors suppress formalin-induced pain through peripheral cannabinoid receptor 1 and cannabinoid receptor 2 receptor mechanisms. MGL inhibition increases paw skin 2-arachidonoylglycerol accumulation to mediate these effects
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MGLL_RAT
303
0
33500
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
two closely related isoforms of 35000 Da and 37000 Da, SDS-PAGE
37000
two closely related isoforms of 35000 Da and 37000 Da, SDS-PAGE
35000
37000
35000
-
x * 35000, brain splicing variant isozyme 1, SDS-PAGE, x * 37000, brain splicing variant isozyme 1, SDS-PAGE
37000
-
x * 35000, brain splicing variant isozyme 1, SDS-PAGE, x * 37000, brain splicing variant isozyme 1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
structure molecular modeling from amino acid sequence
?
-
x * 35000, brain splicing variant isozyme 1, SDS-PAGE, x * 37000, brain splicing variant isozyme 1, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C201G
-
causes significant decreases in enzyme activity, albeit smaller than that produced by mutant C242G. Inhibitory potency of N-arachidonylmaleimide is selectively decreased
C208G
-
causes significant decreases in enzyme activity, albeit smaller than that produced by mutant C242G. Inhibitory potency of octhilinone is selectively decreased. Has no effect on the inhibitory potency of N-arachidonylmaleimide
C242G
-
produces a striking reduction in MGL activity, due to a decrease in maximal reaction velocity rather than a change in Michaelis constant. Inhibitory potency of N-arachidonylmaleimide is selectively decreased
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol, 2 weeks, 25% loss of activity of the plasma membrane enzyme, no loss of activity of the cytosolic enzyme
-
-70°C, 20 mM Tris-HCl or phosphate buffer, pH 7.0, 1 mM dithiothreitol, 1 mM EDTA, 0.2% C13E12, stable for several months
-
4°C, 20 mM Tris-HCl or phosphate buffer, pH 7.0, 1 mM dithiothreitol, 1 mM EDTA, 0.2% C13E12, half-life: 9 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length cDNA subcloned into the pEF15b vector containing an N-terminal histidine tag and transformed in Escherichia coli DH5alpha. Positive clones expressed in Escherichia coli Rosetta 2(De3)pLysS cells. Expression of wild-type and mutants in HeLa cells
-
HeLa cells transiently transfected with pEF6 vector containing full-length ABHD6 or ABHD12
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
selective inhibitors of MGL may be valuable novel agents for the treatment of inflammatory pain. (2S,9Z)-octadec-9-ene-1,2-diamine is a selective inhibitor of MGL activity with in vivo analgesic and anti-inflammatory properties
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Karlsson, M.; Contreras, J.A.; Hellman, U.; Tornqvist, H.; Holm, C.
cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase
J. Biol. Chem.
272
27218-27223
1997
Mus musculus, Rattus norvegicus
Fredrikson, G.; Tornqvist, H.; Belfrage, P.
Hormone-sensitive lipase and monoacylglycerol lipase are both required for complete degradation of adipocyte triacylglycerol
Biochim. Biophys. Acta
876
288-293
1986
Rattus norvegicus
Errasfa, M.
Characterization of several phospholipase activities and diacylglycerol/2-monoacylglycerol lipases in rat alveolar macrophages
Biochim. Biophys. Acta
1085
201-208
1991
Rattus norvegicus
Konrad, R.J.; Major, C.D.; Wolf, B.A.
Diacylglycerol hydrolysis to arachidonic acid is necessary for insulin secretion from isolated pancreatic islets: sequential actions of diacylglycerol and monoacylglycerol lipases
Biochemistry
33
13284-13294
1994
Rattus norvegicus
Sakurada, T.; Noma, A.
Subcellular localization and some properties of monoacylglycerol lipase in rat adipocytes
J. Biochem.
90
1413-1419
1981
Rattus norvegicus
Tornqvist, H.; Belfrage, P.
Monoacylglycerol lipase from rat adipose tissue
Methods Enzymol.
71
647-652
1981
Rattus norvegicus
-
De Jong, B.J.P.; Kalkman, C.; Hulsmann, W.C.
Partial purification and properties of monoacylglycerol lipase and two esterases from isolated rat small intestinal epithelial cells
Biochim. Biophys. Acta
530
56-66
1978
Rattus norvegicus
Ikeda, Y.; Okamura, K.; Fujii, S.
Purification and characterization of rat liver microsomal monoacylglycerol lipase in comparison to the other esterases
Biochim. Biophys. Acta
488
128-139
1977
Rattus norvegicus
Saario, S.M.; Savinainen, J.R.; Laitinen, J.T.; Jarvinen, T.; Niemi, R.
Monoglyceride lipase-like enzymatic activity is responsible for hydrolysis of 2-arachidonoylglycerol in rat cerebellar membranes
Biochem. Pharmacol.
67
1381-1387
2004
Rattus norvegicus
Dinh, T.P.; Freund, T.F.; Piomelli, D.
A role for monoglyceride lipase in 2-arachidonoylglycerol inactivation
Chem. Phys. Lipids
121
149-158
2002
Rattus norvegicus
Ito, M.; Tchoua, U.; Okamoto, M.; Tojo, H.
Purification and properties of a phospholipase A2/lipase preferring phosphatidic acid, bis(monoacylglycerol) phosphate, and monoacylglycerol from rat testis
J. Biol. Chem.
277
43674-43681
2002
Rattus norvegicus
Dinh, T.P.; Carpenter, D.; Leslie, F.M.; Freund, T.F.; Katona, I.; Sensi, S.L.; Kathuria, S.; Piomelli, D.
Brain monoglyceride lipase participating in endocannabinoid inactivation
Proc. Natl. Acad. Sci. USA
99
10819-10824
2002
Rattus norvegicus (Q8R431)
Vandevoorde, S.; Saha, B.; Mahadevan, A.; Razdan, R.K.; Pertwee, R.G.; Martin, B.R.; Fowler, C.J.
Influence of the degree of unsaturation of the acyl side chain upon the interaction of analogues of 1-arachidonoylglycerol with monoacylglycerol lipase and fatty acid amide hydrolase
Biochem. Biophys. Res. Commun.
337
104-109
2005
Rattus norvegicus
Ghafouri, N.; Tiger, G.; Razdan, R.K.; Mahadevan, A.; Pertwee, R.G.; Martin, B.R.; Fowler, C.J.
Inhibition of monoacylglycerol lipase and fatty acid amide hydrolase by analogues of 2-arachidonoylglycerol
Br. J. Pharmacol.
143
774-784
2004
Rattus norvegicus
Vandevoorde, S.; Fowler, C.J.
Inhibition of fatty acid amide hydrolase and monoacylglycerol lipase by the anandamide uptake inhibitor VDM11: evidence that VDM11 acts as an FAAH substrate
Br. J. Pharmacol.
145
885-893
2005
Rattus norvegicus
Saario, S.M.; Salo, O.M.; Nevalainen, T.; Poso, A.; Laitinen, J.T.; Jarvinen, T.; Niemi, R.
Characterization of the sulfhydryl-sensitive site in the enzyme responsible for hydrolysis of 2-arachidonoyl-glycerol in rat cerebellar membranes
Chem. Biol.
12
649-656
2005
Rattus norvegicus (Q8R431)
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
Vila, A.; Rosengarth, A.; Piomelli, D.; Cravatt, B.; Marnett, L.J.
Hydrolysis of prostaglandin glycerol esters by the endocannabinoid-hydrolyzing enzymes, monoacylglycerol lipase and fatty acid amide hydrolase
Biochemistry
46
9578-9585
2007
Rattus norvegicus
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
Hashimotodani, Y.; Ohno-Shosaku, T.; Kano, M.
Presynaptic monoacylglycerol lipase activity determines basal endocannabinoid tone and terminates retrograde endocannabinoid signaling in the hippocampus
J. Neurosci.
27
1211-1219
2007
Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
Duncan, M.; Thomas, A.D.; Cluny, N.L.; Patel, A.; Patel, K.D.; Lutz, B.; Piomelli, D.; Alexander, S.P.; Sharkey, K.A.
Distribution and function of monoacylglycerol lipase in the gastrointestinal tract
Am. J. Physiol. Gastrointest. Liver Physiol.
295
G1255-G1265
2008
Mus musculus, Rattus norvegicus
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
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
Magrioti, V.; Naxakis, G.; Hadjipavlou-Litina, D.; Makriyannis, A.; Kokotos, G.
A novel monoacylglycerol lipase inhibitor with analgesic and anti-inflammatory activity
Bioorg. Med. Chem. Lett.
18
5424-5427
2008
Rattus norvegicus
King, A.R.; Lodola, A.; Carmi, C.; Fu, J.; Mor, M.; Piomelli, D.
A critical cysteine residue in monoacylglycerol lipase is targeted by a new class of isothiazolinone-based enzyme inhibitors
Br. J. Pharmacol.
157
974-983
2009
Rattus norvegicus
King, A.R.; Dotsey, E.Y.; Lodola, A.; Jung, K.M.; Ghomian, A.; Qiu, Y.; Fu, J.; Mor, M.; Piomelli, D.
Discovery of potent and reversible monoacylglycerol lipase inhibitors
Chem. Biol.
16
1045-1052
2009
Rattus norvegicus
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
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
Guindon, J.; Guijarro, A.; Piomelli, D.; Hohmann, A.G.
Peripheral antinociceptive effects of inhibitors of monoacylglycerol lipase in a rat model of inflammatory pain
Br. J. Pharmacol.
163
1464-1478
2011
Rattus norvegicus
Berdan, C.A.; Erion, K.A.; Burritt, N.E.; Corkey, B.E.; Deeney, J.T.
Inhibition of monoacylglycerol lipase activity decreases glucose-stimulated insulin secretion in INS-1 (832/13) cells and rat islets
PLoS ONE
11
e0149008
2016
Rattus norvegicus (Q8R431), Rattus norvegicus Sprague-Dawley (Q8R431)
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