PNPLA3 Protein, Human (I148M, sf9, His)

PNPLA3 specifically catalyzes the coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to produce phosphatidic acid (PA), a key metabolic intermediate and precursor for both triglycerides and glycerophospholipids. It does not esterify other lysophospholipids, utilizing long-chain (at least C16) fatty acyl-CoAs such as arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA, and to a lesser extent, palmitoyl-CoA as acyl donors. Additionally, PNPLA3 exhibits low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities, suggesting a potential role in triglyceride acyl-chain remodeling. In vitro studies indicate hydrolytic activity against triacylglycerol, diacylglycerol, and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety. However, its triacylglycerol hydrolase activity is debated and may be minimal. PNPLA3 also possesses phospholipase A2 activity. by similar: The enzyme's activity varies across studies, particularly regarding the extent of its triacylglycerol hydrolase function.