Diacylglycerol lipase

diacylglycerol lipase β
diacylglycerol lipase β
	DAGLβ structure, folded with AlphaFold. Transmembrane domain in marine blue. Catalytic domain in yellow. Note missing C-terminal tail. See Structure for details. Click image for higher resolution.
Identifiers
Symbol	DAGLB
NCBI gene	221955
HGNC	28923
RefSeq	NM_139179
UniProt	Q8NCG7
Other data
EC number	3.1.1.116
Locus	Chr. 7 p22.1
Structures
Search for
Structures	Swiss-model
Domains	InterPro

Search for
Structures	Swiss-model
Domains	InterPro

diacylglycerol lipase α
diacylglycerol lipase α
	DAGLα structure, folded with AlphaFold. Transmembrane domain in marine blue. Catalytic domain in yellow. C-terminal tail in gray. See Structure for details. Click image for higher resolution.
Identifiers
Symbol	DAGLA
Alt. symbols	C11orf11
NCBI gene	747
HGNC	1165
RefSeq	NM_006133
UniProt	Q9Y4D2
Other data
EC number	3.1.1.116
Locus	Chr. 11 q12.3
Structures
Search for
Structures	Swiss-model
Domains	InterPro

Diacylglycerol lipase, also known as DAG lipase, DAGL, or DGL, is an enzyme that catalyzes the hydrolysis of diacylglycerol, releasing a free fatty acid and monoacylglycerol:^[1]

diacylglycerol + H₂O ⇌ monoacylglycerol + free fatty acid

DAGL has been studied in multiple domains of life, including bacteria, fungi, plants, insects, and mammals.^[4] By searching with BLAST for the previously sequenced microorganism DAGL,^[5] Bisogno et al discovered two distinct mammalian isoforms, designated DAGLα (DAGLA) and DAGLβ (DAGLB).^[1] Most animal DAGL enzymes cluster into the DAGLα and DAGLβ isoforms.^[4]

Mammalian DAGL is a crucial enzyme in the biosynthesis of 2-arachidonoylglycerol (2-AG), the most abundant endocannabinoid in tissues.^[1] The endocannabinoid system has been identified to have considerable involvement in the regulation of homeostasis and disease.^[6] As a result, much effort has been made toward investigating the mechanisms of action and the therapeutic potential of the system's receptors, endogenous ligands, and enzymes like DAGLα and DAGLβ.^[6]

^ ^a ^b ^c ^d ^e Bisogno T, Howell F, Williams G, et al. (November 2003). "Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain". J. Cell Biol. 163 (3): 463–8. doi:10.1083/jcb.200305129. PMC 2173631. PMID 14610053.
^ ^a ^b Jumper, John; Evans, Richard; Pritzel, Alexander; Green, Tim; Figurnov, Michael; Ronneberger, Olaf; Tunyasuvunakool, Kathryn; Bates, Russ; Žídek, Augustin; Potapenko, Anna; Bridgland, Alex; Meyer, Clemens; Kohl, Simon A. A.; Ballard, Andrew J.; Cowie, Andrew (2021-07-15). "Highly accurate protein structure prediction with AlphaFold". Nature. 596 (7873): 583–589. Bibcode:2021Natur.596..583J. doi:10.1038/s41586-021-03819-2. ISSN 1476-4687. PMC 8371605. PMID 34265844.
^ ^a ^b Mirdita, Milot; Schütze, Konstantin; Moriwaki, Yoshitaka; Heo, Lim; Ovchinnikov, Sergey; Steinegger, Martin (2022-05-30). "ColabFold: making protein folding accessible to all". Nature Methods. 19 (6): 679–682. doi:10.1038/s41592-022-01488-1. ISSN 1548-7105. PMC 9184281. PMID 35637307.
^ ^a ^b Yuan, Dongjuan; Wu, Zhongdao; Wang, Yonghua (2016-08-26). "Evolution of the diacylglycerol lipases". Progress in Lipid Research. 64: 85–97. doi:10.1016/j.plipres.2016.08.004. ISSN 1873-2194. PMID 27568643.
^ Yamaguchi, Shotaro; Tamio, Mase; Kazuyuki, Takeuchi (1991-07-15). "Cloning and structure of the mono- and diacylglycerol lipase-encoding gene from Penicillium camembertii U-150". Gene. 103 (1): 61–67. doi:10.1016/0378-1119(91)90391-N. ISSN 0378-1119. PMID 1879699.
^ ^a ^b Wilkerson, Jenny L.; Bilbrey, Joshua A.; Felix, Jasmine S.; Makriyannis, Alexandros; McMahon, Lance R. (2021-04-29). "Untapped endocannabinoid pharmacological targets: Pipe dream or pipeline?". Pharmacology, Biochemistry, and Behavior. 206: 173192. doi:10.1016/j.pbb.2021.173192. ISSN 1873-5177. PMID 33932409. S2CID 233477096.

[Bisogno_2003-1] Bisogno T, Howell F, Williams G, et al. (November 2003). "Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain". J. Cell Biol. 163 (3): 463–8. doi:10.1083/jcb.200305129. PMC 2173631. PMID 14610053.

[AlphaFold_2021-2] Jumper, John; Evans, Richard; Pritzel, Alexander; Green, Tim; Figurnov, Michael; Ronneberger, Olaf; Tunyasuvunakool, Kathryn; Bates, Russ; Žídek, Augustin; Potapenko, Anna; Bridgland, Alex; Meyer, Clemens; Kohl, Simon A. A.; Ballard, Andrew J.; Cowie, Andrew (2021-07-15). "Highly accurate protein structure prediction with AlphaFold". Nature. 596 (7873): 583–589. Bibcode:2021Natur.596..583J. doi:10.1038/s41586-021-03819-2. ISSN 1476-4687. PMC 8371605. PMID 34265844.

[ColabFold_2022-3] Mirdita, Milot; Schütze, Konstantin; Moriwaki, Yoshitaka; Heo, Lim; Ovchinnikov, Sergey; Steinegger, Martin (2022-05-30). "ColabFold: making protein folding accessible to all". Nature Methods. 19 (6): 679–682. doi:10.1038/s41592-022-01488-1. ISSN 1548-7105. PMC 9184281. PMID 35637307.

[Yuan_2016-4] Yuan, Dongjuan; Wu, Zhongdao; Wang, Yonghua (2016-08-26). "Evolution of the diacylglycerol lipases". Progress in Lipid Research. 64: 85–97. doi:10.1016/j.plipres.2016.08.004. ISSN 1873-2194. PMID 27568643.

[Yamaguchi_1991-5] Yamaguchi, Shotaro; Tamio, Mase; Kazuyuki, Takeuchi (1991-07-15). "Cloning and structure of the mono- and diacylglycerol lipase-encoding gene from Penicillium camembertii U-150". Gene. 103 (1): 61–67. doi:10.1016/0378-1119(91)90391-N. ISSN 0378-1119. PMID 1879699.

[:0-6] Wilkerson, Jenny L.; Bilbrey, Joshua A.; Felix, Jasmine S.; Makriyannis, Alexandros; McMahon, Lance R. (2021-04-29). "Untapped endocannabinoid pharmacological targets: Pipe dream or pipeline?". Pharmacology, Biochemistry, and Behavior. 206: 173192. doi:10.1016/j.pbb.2021.173192. ISSN 1873-5177. PMID 33932409. S2CID 233477096.

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