Abstract
The covalent attachment of long chain fatty acids to proteins was first described for brain myelin proteolipoprotein (15). The major membrane lipoprotein in the Escherichia coli cell wall was later shown to contain fatty acids attached through both ester and amide linkages (6, 19). This covalent modification has been subsequently shown to be common to a variety of eukaryotic, bacterial, and viral membrane glycoproteins. However, fatty acid acylation is a highly selective modification, even among membrane glycoproteins, since only a subset of membrane-associated proteins contain lipids. Because fatty acylation is such a recently identified covalent modification, the characteristics of a protein that specify whether it becomes acylated, as well as the biosynthetic events involved in the attachment of fatty acids to proteins, are only beginning to be explored. This review will summarize current knowledge regarding this unique covalent modification and will discuss possible avenues of future research that might provide a clearer understanding of the structure, function, and biosynthesis of fatty acid-acylated proteins.
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Olson, E.N. (1986). Structure, Function, and Biosynthesis of Fatty Acid-Acylated Proteins. In: Strauss, A.W., Boime, I., Kreil, G. (eds) Protein Compartmentalization. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4930-6_6
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DOI: https://doi.org/10.1007/978-1-4612-4930-6_6
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