Enzyme specificity as a factor in regulation of fatty acid chain length in Escherichia coli.
Various acyl-acyl carrier protein intermediates in saturated and unsaturated fatty acid biosynthesis were tested as substrates for beta-ketoacyl-acyl carrier protein synthetase. With both classes of substrates the condensing enzyme in fatty biosynthesis demonstrates specificities which indicate that it might be an important factor in determining fatty acid chain length in Escherichia coli.
D000217:Acyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D002247:Carbon Isotopes; D004926:Escherichia coli / Q000201:enzymology*; D005227:Fatty Acids / Q000096:biosynthesis*; D007651:Keto Acids; D007700:Kinetics; D008314:Malonates
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D005227:Fatty Acids; D007651:Keto Acids; D008314:Malonates; D000217:Acyltransferases