Topic
Patatin-like phospholipase
About: Patatin-like phospholipase is a research topic. Over the lifetime, 55 publications have been published within this topic receiving 2469 citations. The topic is also known as: Patatin-like phospholipase domain, protein family & IPR002641.
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TL;DR: Three novel TAG lipases/acylglycerol transacylases that likely participate in TAG hydrolysis and the acyl-CoA independent transacylation of acylglycerols, thereby facilitating energy mobilization and storage in adipocytes are identified.
805 citations
TL;DR: C cumulative data suggest that patatin-like genes normally expressed at very low levels are induced in response to environmental signals, and a single nomenclature to describe the PNPLA family is proposed.
271 citations
TL;DR: The human genome expresses nine patatin-like phospholipase domain containing proteins (PNPLA1-9) as mentioned in this paper, which share a protein domain discovered initially in patatin, the most abundant protein of the potato tuber.
259 citations
TL;DR: The X-ray crystal structure of a His-tagged variant of an isozyme of patatin, Pat17, is determined, revealing that patatin has a Ser-Asp catalytic dyad and an active site like that of human cytosolic phospholipase A(2) (cPLA(2))
Abstract: Patatin is a nonspecific lipid acyl hydrolase that accounts for approximately 40% of the total soluble protein in mature potato tubers, and it has potent insecticidal activity against the corn rootworm. We determined the X-ray crystal structure of a His-tagged variant of an isozyme of patatin, Pat17, to 2.2 A resolution, employing SeMet multiwavelength anomalous dispersion (MAD) phasing methods. The patatin crystal structure has three molecules in the asymmetric unit, an R-factor of 22.0%, and an Rfree of 27.2% (for 10% of the data not included in the refinement) and includes 498 water molecules. The structure notably revealed that patatin has a Ser-Asp catalytic dyad and an active site like that of human cytosolic phospholipase A2 (cPLA2) [Dessen, A., et al. (1999) Cell 97, 349−360]. In addition, patatin has a folding topology related to that of the catalytic domain of cPLA2 and unlike the canonical α/β-hydrolase fold. The structure confirms our site-directed mutagenesis and bioactivity data that initial...
258 citations
TL;DR: Loss of Pnpla3 does not cause fatty liver, liver enzyme elevation, or insulin resistance in mice, and mice displayed similar glucose tolerance and insulin tolerance tests while on regular chow or three different fatty liver–inducing diets.
205 citations