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( R e d i r e c t e d f r o m A c y l g l y c e r o l l i p a s e )
Monoacylglycerol lipase (EC 3.1.1.23; systematic name glycerol-ester acylhydrolase , also known as MAG lipase , acylglycerol lipase , MAGL , MGL or MGLL ) is an enzyme that, in humans, is encoded by the MGLL gene .[1] [2] [3] serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239.[2] [4]
Human monoacylglycerol lipase
Function
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Monoacylglycerol lipase catalyzes a reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids :
hydrolyses glycerol monoesters of long-chain fatty acids
It functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.[5]
Monoacylglycerol lipase is a key enzyme in the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-AG).[6] [7] monoacylglycerols to the free fatty acid and glycerol . The contribution of MAGL to total brain 2-AG hydrolysis activity has been estimated to be ~85% (ABHD6 and ABHD12 are responsible for ~4% and ~9%, respectively, of the remainder),[8] [9] in vitro estimate has been confirmed in vivo by the selective MAGL inhibitor JZL184 .[10] downregulation of CB1 [11]
Inhibitors
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MAGL enzyme inhibitors (URB602 , URB754 , JZL184 ) produce cannabinoid behavioral effects in mice.[10]
Further examples include:[citation needed
KML-29
JZL195
JNJ-42165279
JW 642
See also
[ edit ]
References
[ edit ]
^ Wall EM, Cao J, Chen N, Buller RM, Upton C (December 1997). "A novel poxvirus gene and its human homolog are similar to an E. coli lysophospholipase". Virus Research . 52 2 ): 157–67. doi :10.1016/S0168-1702(97 )00122-6 . PMID 9495531 .
^ a b Karlsson M, Contreras JA, Hellman U, Tornqvist H, Holm C (October 1997). "cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases" . The Journal of Biological Chemistry . 272 (43 ): 27218–23. doi :10.1074/jbc.272.43.27218 PMID 9341166 .
^ "Entrez Gene: monoglyceride lipase" .
^ Tornqvist H, Belfrage P (February 1976). "Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue" . The Journal of Biological Chemistry . 251 (3 ): 813–9. doi :10.1016/S0021-9258(17 )33857-7 PMID 1249056 .
^ Karlsson M, Reue K, Xia YR, Lusis AJ, Langin D, Tornqvist H, Holm C (July 2001). "Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene". Gene . 272 (1–2): 11–8. doi :10.1016/S0378-1119(01 )00559-5 . PMID 11470505 .
^ Dinh TP, Carpenter D, Leslie FM, Freund TF, Katona I, Sensi SL, Kathuria S, Piomelli D (August 2002). "Brain monoglyceride lipase participating in endocannabinoid inactivation" . Proceedings of the National Academy of Sciences of the United States of America . 99 16 ): 10819–24. Bibcode :2002PNAS...9910819D . doi :10.1073/pnas.152334899 PMC 125056 PMID 12136125 .
^ Makara JK, Mor M, Fegley D, Szabó SI, Kathuria S, Astarita G, Duranti A, Tontini A, Tarzia G, Rivara S, Freund TF, Piomelli D (September 2005). "Selective inhibition of 2-AG hydrolysis enhances endocannabinoid signaling in hippocampus" . Nature Neuroscience . 8 9 ): 1139–41. doi :10.1038/nn1521 PMID 16116451 . S2CID 52810445 .
^ Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief ISBN 978-1-4816-0672-1
^ Blankman JL, Simon GM, Cravatt BF (December 2007). "A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol" . Chemistry & Biology . 14 12 ): 1347–56. doi :10.1016/j.chembiol.2007.11.006 . PMC 2692834 PMID 18096503 .
^ a b Long JZ, Li W, Booker L, Burston JJ, Kinsey SG, Schlosburg JE, Pavón FJ, Serrano AM, Selley DE, Parsons LH, Lichtman AH, Cravatt BF (January 2009). "Selective blockade of 2-arachidonoylglycerol hydrolysis produces cannabinoid behavioral effects" . Nature Chemical Biology . 5 1 ): 37–44. doi :10.1038/nchembio.129 . PMC 2605181 PMID 19029917 .
^ Savinainen JR, Saario SM, Laitinen JT (February 2012). "The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors" . Acta Physiologica . 204 (2 ): 267–76. doi :10.1111/j.1748-1716.2011.02280.x . PMC 3320662 PMID 21418147 .
External links
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This article incorporates text from the United States National Library of Medicine , which is in the public domain .
t
e
Receptor (ligands )
CB 1 Tooltip Cannabinoid receptor type 1
Agonists(abridged,full list )
Inverse agonists
Antagonists
CB 2 Tooltip Cannabinoid receptor type 2
Agonists
2-AG
2-AGE (noladin ether)
3,3'-Diindolylmethane
4-O-Methylhonokiol
α-Amyrin · β-Amyrin
A-796,260
A-834,735
A-836,339
AM-1172
AM-1221
AM-1235
AM-1241
AM-2232
Anandamide
AZ-11713908
Cannabinol
Caryophyllene
CB-13
CBS-0550
CP 55,940
GW-405,833 (L-768,242)
GW-842,166X
HU-308
JTE 7-31
JWH-007
JWH-015
JWH-018
JWH-73
JWH-133
L-759,633
L-759,656
Lenabasum (anabasum)
Magnolol
MDA-19
Nabitan
NADA
Olorinab (APD-371)
PF-03550096
S-444,823
SER-601
Serinolamide A
UR-144
Tedalinab
THC (dronabinol)
THCV
Tetrahydromagnolol
Virodhamine
Antagonists
NAGly GPR18 )
GPR55
GPR119
Transporter (modulators )
eCBTs Tooltip Endocannabinoid transporter
Enzyme (modulators )
Others
Others: 2-PG (directly potentiates activity of 2-AG at CB1
ARN-272 (FAAH-like anandamide transporter inhibitor)
See also
Receptor/signaling modulators
Cannabinoids (cannabinoids by structure)
R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Monoacylglycerol_lipase&oldid=1215943647 " C a t e g o r i e s : ● G e n e s o n h u m a n c h r o m o s o m e 3 ● E C 3 . 1 . 1 ● E n z y m e s o f u n k n o w n s t r u c t u r e H i d d e n c a t e g o r i e s : ● A r t i c l e s w i t h s h o r t d e s c r i p t i o n ● S h o r t d e s c r i p t i o n m a t c h e s W i k i d a t a ● P r o t e i n p a g e s n e e d i n g a p i c t u r e ● A l l a r t i c l e s w i t h u n s o u r c e d s t a t e m e n t s ● A r t i c l e s w i t h u n s o u r c e d s t a t e m e n t s f r o m M a r c h 2 0 2 4 ● W i k i p e d i a a r t i c l e s i n c o r p o r a t i n g t e x t f r o m t h e U n i t e d S t a t e s N a t i o n a l L i b r a r y o f M e d i c i n e
● T h i s p a g e w a s l a s t e d i t e d o n 2 8 M a r c h 2 0 2 4 , a t 0 2 : 2 2 ( U T C ) . ● T e x t i s a v a i l a b l e u n d e r t h e C r e a t i v e C o m m o n s A t t r i b u t i o n - S h a r e A l i k e L i c e n s e 4 . 0 ;
a d d i t i o n a l t e r m s m a y a p p l y . B y u s i n g t h i s s i t e , y o u a g r e e t o t h e T e r m s o f U s e a n d P r i v a c y P o l i c y . W i k i p e d i a ® i s a r e g i s t e r e d t r a d e m a r k o f t h e W i k i m e d i a F o u n d a t i o n , I n c . , a n o n - p r o f i t o r g a n i z a t i o n . ● P r i v a c y p o l i c y ● A b o u t W i k i p e d i a ● D i s c l a i m e r s ● C o n t a c t W i k i p e d i a ● C o d e o f C o n d u c t ● D e v e l o p e r s ● S t a t i s t i c s ● C o o k i e s t a t e m e n t ● M o b i l e v i e w
