DAG is hydrolyzed to 2-MAG by PNPLA2/3

Stable Identifier
R-HSA-1482811
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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At the endoplasmic reticulum (ER) membrane, patatin-like phospholipase domain-containing proteins 2/3 (PNPLA2/3) hydrolyze diacylglycerol (DAG), removing an acyl group to form 2-monoacylglycerol (2-MAG) (He et al. 2010, Jenkins et al. 2004, Basantani et al. 2011).

Literature References
PubMed ID Title Journal Year
20034933 A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis

He, S, McPhaul, C, Li, JZ, Garuti, R, Kinch, L, Grishin, NV, Cohen, JC, Hobbs, HH

J Biol Chem 2010
21068004 Pnpla3/Adiponutrin deficiency in mice does not contribute to fatty liver disease or metabolic syndrome

Basantani, MK, Sitnick, MT, Cai, L, Brenner, DS, Gardner, NP, Li, JZ, Schoiswohl, G, Yang, K, Kumari, M, Gross, RW, Zechner, R, Kershaw, EE

J Lipid Res 2011
15364929 Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities

Jenkins, CM, Mancuso, DJ, Yan, W, Sims, HF, Gibson, B, Gross, RW

J Biol Chem 2004
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
lipoprotein lipase activity of PNPLA2/3 [endoplasmic reticulum membrane]
Physical Entity
Activity
Orthologous Events
Authored
Created