7ots

Structural highlights

Function

ABHD6_HUMAN Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol (PubMed:22969151). Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting (PubMed:26491015).[UniProtKB:Q8R2Y0]^{[1] [2]}

See Also

• Lipase 3D Structures

References

1. ↑ Navia-Paldanius D, Savinainen JR, Laitinen JT. Biochemical and pharmacological characterization of human alpha/beta-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12). J Lipid Res. 2012 Nov;53(11):2413-24. doi: 10.1194/jlr.M030411. Epub 2012 Sep 11. PMID:22969151 doi:http://dx.doi.org/10.1194/jlr.M030411
2. ↑ Pribasnig MA, Mrak I, Grabner GF, Taschler U, Knittelfelder O, Scherz B, Eichmann TO, Heier C, Grumet L, Kowaliuk J, Romauch M, Holler S, Anderl F, Wolinski H, Lass A, Breinbauer R, Marsche G, Brown JM, Zimmermann R. alpha/beta Hydrolase Domain-containing 6 (ABHD6) Degrades the Late Endosomal/Lysosomal Lipid Bis(monoacylglycero)phosphate. J Biol Chem. 2015 Dec 11;290(50):29869-81. doi: 10.1074/jbc.M115.669168. Epub, 2015 Oct 21. PMID:26491015 doi:http://dx.doi.org/10.1074/jbc.M115.669168