Purification and positional specificity of sn-glycerol-3-phosphate acyltransferase from Escherichia coli membranes.
SN-Glycerol-3-phosphate acyltransferase was solubilized from membranes of Escherichia coli B and K-12 and purified on an affinity column of Sepharose 4B coupled with 6-phosphogluconic acid. Phosphatidylglycerol was required for activation and stabilization of the purified enzyme. The acyl residues were exclusively transferred to the position 1 of sn-glycerol 3-phosphate by the enzyme, regardless of whether the acyl-CoA was saturated or unsaturated.
D000217:Acyltransferases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology*; D002846:Chromatography, Affinity; D003065:Coenzyme A / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005227:Fatty Acids / Q000378:metabolism; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000302:isolation & purification / Q000378:metabolism*; D005994:Glycerophosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010715:Phosphatidylglycerols / Q000494:pharmacology; D013329:Structure-Activity Relationship
D005227:Fatty Acids; D005994:Glycerophosphates; D010715:Phosphatidylglycerols; D000217:Acyltransferases; D005992:Glycerol-3-Phosphate O-Acyltransferase; D003065:Coenzyme A