Effects of palmitoyl-CoA on the structure-function of the fatty acid synthetase complex from Ceratitis capitata.
1. The effects of palmitoyl-CoA on the structure and enzyme activity of the fatty acid synthetase from the insect Ceratitis capitata have been examined. 2. The acyl-CoA derivative increases the helical content of the protein from 45 to 60% and inhibits the enzyme activity of the complex. 3. Bovine serum albumin, calf thymus histone H1 and phospholipids protect the enzyme from the inactivation by palmitoyl-CoA. Phospholipids increase also the ellipticity at 220 nm in the enzyme complex. 4. The results obtained show a non specific character for the inhibition and are interpreted in terms of the detergent properties of the long-chain acyl-CoA derivatives.
D000214:Acyl Coenzyme A / Q000494:pharmacology*; D000818:Animals; D004175:Diptera / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D064429:Fatty Acid Synthases / Q000037:antagonists & inhibitors*; D006657:Histones / Q000494:pharmacology; D010171:Palmitoyl Coenzyme A / Q000494:pharmacology*; D010743:Phospholipids / Q000494:pharmacology; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D013329:Structure-Activity Relationship
D000214:Acyl Coenzyme A; D006657:Histones; D010743:Phospholipids; D010171:Palmitoyl Coenzyme A; D012710:Serum Albumin, Bovine; D064429:Fatty Acid Synthases