Phosphatidic acid synthesis in Escherichia coli.
The kinetic properties of acyl-coenzyme A (CoA): l-alpha-glycerol-phosphate trans-acylase (EC 2.3.1.15) from Escherichia coli were studied. At 10 C, a temperature at which the reaction was proportional to time and enzyme concentration, the enzyme had an apparent K(m) of 60 mum for l-alpha-glycerol-phosphate. The curve describing the velocity of the reaction as a function of palmitoyl-CoA concentration was sigmoid but the plot of v(-1) versus [S](-3) gave a straight line. A K(m) of about 11 mum was calculated for palmitoyl-CoA. Adenosine triphosphate specifically inhibited the reaction, being a noncompetitive inhibitor in respect to l-alpha-glycerol phosphate. Inhibition only occurred with high concentrations of palmitoyl-CoA, and maximal inhibition was 60%.
D000217:Acyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D002247:Carbon Isotopes; D002854:Chromatography, Paper; D002855:Chromatography, Thin Layer; D003065:Coenzyme A / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D005994:Glycerophosphates / Q000378:metabolism; D007700:Kinetics; D009711:Nucleotides / Q000494:pharmacology; D010743:Phospholipids / Q000096:biosynthesis* / Q000378:metabolism; D010759:Phosphorus Isotopes
D002247:Carbon Isotopes; D005994:Glycerophosphates; D009711:Nucleotides; D010743:Phospholipids; D010759:Phosphorus Isotopes; D000255:Adenosine Triphosphate; D000217:Acyltransferases; D003065:Coenzyme A