The Palmityl Binding Sites of Fatty Acid Synthetase from Yeast

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Abstract
Fatty acid synthetase was covalently labelled with [14C]palmitic acid from [14C]palmityl‐CoA. Tryptic and peptic digestion of the [14C]palmityl enzyme resulted in the formation of radioactive palmityl peptides carrying the long‐chain acyl residue both in oxygen‐ester and thio‐ester linkage. The lipophilic palmityl peptides were purified by column and thin‐layer chromatography using organic solvent systems. peptides arising from the acyl carrier protein, the condensing enzyme and the palmityl transferase were identified and characterized. The amino acid sequence of a 4′‐phosphopantetheine‐containing peptide was established. It comprises 13 residues and shows a high degree of homology with the acyl carrier protein from Escherichia coli. A heptapeptide and an octapeptide from the palmityl transferase active site were partially sequenced. The identical amino acid composition of palmityl transferase and malonyl transferase core peptides is briefly discussed.