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- W1993971214 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." @default.
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- W1993971214 date "1977-10-01" @default.
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- W1993971214 title "The Palmityl Binding Sites of Fatty Acid Synthetase from Yeast" @default.
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- W1993971214 doi "https://doi.org/10.1111/j.1432-1033.1977.tb11850.x" @default.
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