Monoacylglycerol lipase | S33: Prolyl aminopeptidase | IUPHAR/BPS Guide to PHARMACOLOGY

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Monoacylglycerol lipase

Target not currently curated in GtoImmuPdb

Target id: 1399

Nomenclature: Monoacylglycerol lipase

Abbreviated Name: MAGL

Family: S33: Prolyl aminopeptidase, 2-Acylglycerol ester turnover, Hydrolases

Annotation status:  image of an orange circle Annotated and awaiting review. Please contact us if you can help with reviewing.  » Email us

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 303 p13-q13.33 MGLL monoglyceride lipase
Mouse - 319 6 D1 Mgll monoglyceride lipase
Rat - 303 4q34 Mgll monoglyceride lipase
Previous and Unofficial Names
HU-K5 | MGL | MAGL | monoacylglycerol lipase
Database Links
Specialist databases
MEROPS S33.980 (Hs)
Other databases
BRENDA
CATH/Gene3D
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Enzyme
KEGG Gene
OMIM
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Enzyme Reaction
EC Number: 3.1.1.23
Endogenous substrates (Human)
2-oleoyl glycerol = 2-arachidonoylglycerol >> anandamide  [4]

Download all structure-activity data for this target as a CSV file

Inhibitors
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter Reference
JJKK 048 Hs Inhibition 9.3 pIC50 1
pIC50 9.3 [1]
KML29 Hs Inhibition 8.5 pIC50 2
pIC50 8.5 [2]
JZL184 Hs Irreversible inhibition 8.4 pIC50 2
pIC50 8.4 (IC50 3.9x10-9 M) [2]
JZL195 Hs Inhibition 8.4 pIC50 5
pIC50 8.4 (IC50 4x10-9 M) [5]
Description: in vitro assay
MJN110 Hs Inhibition 8.0 pIC50 6
pIC50 8.0 (IC50 9.1x10-9 M) [6]
ABX-1431 Hs Irreversible inhibition 7.8 pIC50 3
pIC50 7.8 (IC50 1.4x10-8 M) [3]
ABX-1431 Mm Irreversible inhibition 7.6 pIC50 3
pIC50 7.6 (IC50 2.7x10-8 M) [3]
View species-specific inhibitor tables

References

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1. Aaltonen N, Savinainen JR, Ribas CR, Rönkkö J, Kuusisto A, Korhonen J, Navia-Paldanius D, Häyrinen J, Takabe P, Käsnänen H et al.. (2013) Piperazine and piperidine triazole ureas as ultrapotent and highly selective inhibitors of monoacylglycerol lipase. Chem. Biol., 20 (3): 379-90. [PMID:23521796]

2. Chang JW, Niphakis MJ, Lum KM, Cognetta 3rd AB, Wang C, Matthews ML, Niessen S, Buczynski MW, Parsons LH, Cravatt BF. (2012) Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates. Chem. Biol., 19 (5): 579-88. [PMID:22542104]

3. Cisar JS, Weber OD, Clapper JR, Blankman JL, Henry CL, Simon GM, Alexander JP, Jones TK, Ezekowitz RAB, O'Neill GP et al.. (2018) Identification of ABX-1431, a Selective Inhibitor of Monoacylglycerol Lipase and Clinical Candidate for Treatment of Neurological Disorders. J. Med. Chem., 61 (20): 9062-9084. [PMID:30067909]

4. Ghafouri N, Tiger G, Razdan RK, Mahadevan A, Pertwee RG, Martin BR, Fowler CJ. (2004) Inhibition of monoacylglycerol lipase and fatty acid amide hydrolase by analogues of 2-arachidonoylglycerol. Br. J. Pharmacol., 143 (6): 774-84. [PMID:15492019]

5. Long JZ, Nomura DK, Vann RE, Walentiny DM, Booker L, Jin X, Burston JJ, Sim-Selley LJ, Lichtman AH, Wiley JL et al.. (2009) Dual blockade of FAAH and MAGL identifies behavioral processes regulated by endocannabinoid crosstalk in vivo. Proc. Natl. Acad. Sci. U.S.A., 106 (48): 20270-5. [PMID:19918051]

6. Niphakis MJ, Cognetta 3rd AB, Chang JW, Buczynski MW, Parsons LH, Byrne F, Burston JJ, Chapman V, Cravatt BF. (2013) Evaluation of NHS carbamates as a potent and selective class of endocannabinoid hydrolase inhibitors. ACS Chem Neurosci, 4 (9): 1322-32. [PMID:23731016]

Contributors

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