ABHD6

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene.

== Function ==

ABHD6 is a serine hydrolyzing enzyme that possesses typical α/β-hydrolase family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours.{{cite journal | vauthors = Li F, Fei X, Xu J, Ji C | title = An unannotated alpha/beta hydrolase superfamily member, ABHD6 differentially expressed among cancer cell lines | journal = Molecular Biology Reports | volume = 36 | issue = 4 | pages = 691–6 | date = April 2009 | pmid = 18360779 | doi = 10.1007/s11033-008-9230-7 | s2cid = 6795598 }}

ABHD6 has been linked to regulation of the endocannabinoid system as it controls the accumulation of 2-arachidonoylglycerol (2-AG) at the cannabinoid receptors.{{cite journal | vauthors = Marrs WR, Blankman JL, Horne EA, Thomazeau A, Lin YH, Coy J, Bodor AL, Muccioli GG, Hu SS, Woodruff G, Fung S, Lafourcade M, Alexander JP, Long JZ, Li W, Xu C, Möller T, Mackie K, Manzoni OJ, Cravatt BF, Stella N | title = The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors | journal = Nature Neuroscience | volume = 13 | issue = 8 | pages = 951–7 | date = August 2010 | pmid = 20657592 | pmc = 2970523 | doi = 10.1038/nn.2601 }}

ABHD6 accounts for about 4% of 2-AG brain hydrolysis.{{cite book|title=Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief|url=https://books.google.com/books?id=QZqtIuUdJnQC&pg=PA68|date=26 December 2012|publisher=ScholarlyEditions|isbn=978-1-4816-0672-1|pages=68–}} Together, monoacylglycerol lipase (MAGL), ABHD12, and ABHD6 control about 99% of 2-AG signalling in the brain,{{cite journal | vauthors = Savinainen JR, Saario SM, Laitinen JT | title = The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors | journal = Acta Physiologica | volume = 204 | issue = 2 | pages = 267–76 | date = February 2012 | pmid = 21418147 | pmc = 3320662 | doi = 10.1111/j.1748-1716.2011.02280.x }} and each enzyme exhibits a distinct subcellular distribution, suggesting that they regulate distinct pools of 2-AG in the nervous system.{{cite journal | vauthors = Blankman JL, Simon GM, Cravatt BF | title = A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol | journal = Chemistry & Biology | volume = 14 | issue = 12 | pages = 1347–56 | date = December 2007 | pmid = 18096503 | pmc = 2692834 | doi = 10.1016/j.chembiol.2007.11.006 }}