Proteins containing this domain are lysophospholipid acyltransferases(LPLATs) such as dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) []and glycerol 3-phosphate acyltransferases GPAT1 and GPAT2 []. They are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as dihydroxyacetone phosphate or glycerol 3-phosphate respectively [].
This entry represents the Glycerol-3-phosphate O-acyltransferase/dihydroxyacetone phosphate acyltransferase (GPAT/DAPAT) family. This entry includes PlsB, a GPAT from E. coli in which membrane synthesis depends on allosteric control of this enzyme. PlsB regulation plays an important role in the phospholipid synthesis pathway and is part of the response to certain stress signals []. In many other bacteria, PlsB is not found, and appears to be replaced by a two enzyme system for 1-acyl-glycerol-3-phosphate biosynthesis, the PlsX/Y system [, ].GPATs are classified into four isoforms in mammals; GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, whereas GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane []. This entry includes the mitochondrial isoform, GPAT1 and GPAT2.Dihydroxyacetonephosphate acyltransferase (DHAPAT) catalyses the first step in the biosynthesis of ether phospholipid plasmalogen, and may play also a significant role in nonether glycerolipid biosynthesis [, ]. In humans, mutations in DHAPAT results in the genetic disorder rhizomelic chondrodysplasia punctata type 2, characterised by rhizomelic shortening of femur and humerus, cataract,and severe mental retardation [].
This entry represents the C-terminal domain of glycerol-3-phosphate acyltransferases (GPATs) and dihydroxyacetone phosphate acyltransferases.Dihydroxyacetonephosphate acyltransferase (DHAPAT) catalyses the first step in the biosynthesis of ether phospholipid plasmalogen, and may play also a significant role in nonether glycerolipid biosynthesis [, ]. In humans, mutations in DHAPAT results in the genetic disorder rhizomelic chondrodysplasia punctata type 2, characterised by rhizomelic shortening of femur and humerus, cataract,and severe mental retardation [].This entry includes PlsB, a GPAT from E. coli in which membrane synthesis depends on allosteric control of this enzyme. PlsB regulation plays an important role in the phospholipid synthesis pathway and is part of the response to certain stress signals []. In many other bacteria, PlsB is not found, and appears to be replaced by a two enzyme system for 1-acyl-glycerol-3-phosphate biosynthesis, the PlsX/Y system [, ].GPATs are classified into four isoforms in mammals; GPAT1 and GPAT2 are localized in the mitochondrial outer membrane, whereas GPAT3 and GPAT4 are localized in the endoplasmic reticulum membrane []. This entry includes the mitochondrial isoform GPAT.
