Numerous eukaryotic cellular and viral proteins can be modified by the covalent attachment of fatty acyl groups. Protein acylation is classified into three types,
viz.,
N-myristoylation, thioester (or ester) -linked acylation, and glycosylphosphatidylinositol-linked acylation. Protein
N-myristoylation involves the co-translational attachment of myristic acid (tetradecanoic acid, C
14 : 0) to
N-terminal glycine residues of various proteins. Myristoyl-CoA : protein
N-myristoyltransferase (NMT) is the enzyme by which the myristoyl group is transferred from myristoyl-CoA thioester to
N-terminal glycine residues of nascent acylproteins.
With consideration to the above, the syntheses of long-chain fatty acid analogs, especially myristic acid analogs, containing oxygen, sulfur, double bonds, triple bonds, aromatic residue, carbonyl, ester, and amide are reviewed. The structure-NMT activity relationship is also eluci-dated by using myristic acid analogs,
N-terminal glycine-attached octapeptides, and
Saccharomyces cervisiae NMT
in vitro. The inhibition of the replication of human immunodeficiency virus-1 by these myristic analogs is briefly discussed.
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