The palmityl binding sites of fatty acid synthetase from yeast.
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 lolvent 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'-phosphopant-etheine-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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002852:Chromatography, Ion Exchange; D002855:Chromatography, Thin Layer; D004590:Electrophoresis, Paper; D064429:Fatty Acid Synthases / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D010169:Palmitic Acids / Q000378:metabolism*; D010171:Palmitoyl Coenzyme A / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000596:Amino Acids; D010169:Palmitic Acids; D010446:Peptide Fragments; D010171:Palmitoyl Coenzyme A; D064429:Fatty Acid Synthases