Function of phosphatidylglycerol molecular species in membranes. Activation of membrane-bound sn-glycerol 3-phosphate acyltransferase in Escherichia coli.
SN-Glycerol 3-phosphate acyltrasferase (EC 2.3.1.15) bound to the elaidate enriched membranes of an unsaturated fatty acid auxotroph of Escherichia coli had a lower specific activity than the acyltrasferase associated with the wild-type membranes. The 1-saturated-2-cis-unsaturated and 1,2-di-cis-unsaturated molecular species of phosphatidylglycerol activated this enzyme. However, these molecular species did not change the original temperature profile obtained by Arrhenius plots of the enzyme activity bound to the elaidate-enriched membranes.
D000217:Acyltransferases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology*; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000378:metabolism*; D007700:Kinetics; D010743:Phospholipids / Q000096:biosynthesis*; D013696:Temperature; D013816:Thermodynamics
D010743:Phospholipids; D000217:Acyltransferases; D005992:Glycerol-3-Phosphate O-Acyltransferase