Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3ʼ-(9Z-octadecenoyl)-1ʼ-sn-glycerol) Identifier CHEBI:139150 Charge -1 Formula C42H78O10P InChIKeyhelp_outline GNCZTBXGLUHKAP-JOZUOZHYSA-M SMILEShelp_outline O(C[C@@H](COP([O-])(=O)OC[C@H](COC(CCCCCCC/C=C\CCCCCCCC)=O)O)O)C(CCCCCCC/C=C\CCCCCCCC)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (9Z)-octadecenoate Identifier CHEBI:30823 (Beilstein: 1913148; CAS: 115-06-0) help_outline Charge -1 Formula C18H33O2 InChIKeyhelp_outline ZQPPMHVWECSIRJ-KTKRTIGZSA-M SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 114 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1ʼ-sn-glycerol) Identifier CHEBI:139152 Charge -1 Formula C24H46O9P InChIKeyhelp_outline FQQQKGAFQIIGLQ-RXWKEIDKSA-M SMILEShelp_outline O(C[C@@H](COP(OC[C@H](CO)O)(=O)[O-])O)C(CCCCCCC/C=C\CCCCCCCC)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:55712 | RHEA:55713 | RHEA:55714 | RHEA:55715 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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alpha/beta hydrolase domain-containing 6 (ABHD6) degrades the late endosomal/lysosomal lipid bis(monoacylglycero)phosphate.
Pribasnig M.A., Mrak I., Grabner G.F., Taschler U., Knittelfelder O., Scherz B., Eichmann T.O., Heier C., Grumet L., Kowaliuk J., Romauch M., Holler S., Anderl F., Wolinski H., Lass A., Breinbauer R., Marsche G., Brown J.M., Zimmermann R.
α/β Hydrolase domain-containing 6 (ABHD6) can act as monoacylglycerol hydrolase and is believed to play a role in endocannabinoid signaling as well as in the pathogenesis of obesity and liver steatosis. However, the mechanistic link between gene function and disease is incompletely understood. Her ... >> More
α/β Hydrolase domain-containing 6 (ABHD6) can act as monoacylglycerol hydrolase and is believed to play a role in endocannabinoid signaling as well as in the pathogenesis of obesity and liver steatosis. However, the mechanistic link between gene function and disease is incompletely understood. Here we aimed to further characterize the role of ABHD6 in lipid metabolism. We show that mouse and human ABHD6 degrade bis(monoacylglycero)phosphate (BMP) with high specific activity. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes/lysosomes, where it plays a key role in the formation of intraluminal vesicles and in lipid sorting. Up to now, little has been known about the catabolism of this lipid. Our data demonstrate that ABHD6 is responsible for ∼ 90% of the BMP hydrolase activity detected in the liver and that knockdown of ABHD6 increases hepatic BMP levels. Tissue fractionation and live-cell imaging experiments revealed that ABHD6 co-localizes with late endosomes/lysosomes. The enzyme is active at cytosolic pH and lacks acid hydrolase activity, implying that it degrades BMP exported from acidic organelles or de novo-formed BMP. In conclusion, our data suggest that ABHD6 controls BMP catabolism and is therefore part of the late endosomal/lysosomal lipid-sorting machinery. << Less
J. Biol. Chem. 290:29869-29881(2015) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.