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The Palmityl Binding Sites of Fatty Acid Synthetase from Yeast.
- Source :
- European Journal of Biochemistry; 10/17/77, Vol. 80 Issue 1, p13-23, 11p
- Publication Year :
- 1977
-
Abstract
- Fatty acid synthetase was covalently labelled with [<superscript>14</superscript>C]palmitic acid from [<superscript>14</superscript>C]palmityl-CoA. Tryptic and peptic digestion of the [<superscript>14</superscript>C]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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 80
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15799817
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1977.tb11850.x