種々の官能基をもつ長鎖脂肪酸の合成とそのミリストイルCoA : タンパク質N-ミリストイルトランスフェラーゼ (NMT) 活性
1994 年 43 巻 6 号 p. 459-469
詳細
1994 年 43 巻 6 号 p. 459-469
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. ProteinN-myristoylation involves the co-translational attachment of myristic acid (tetradecanoic acid, C14 : 0) to N-terminal glycine residues of various proteins. Myristoyl-CoA : proteinN-myristoyltransferase (NMT) is the enzyme by which the myristoyl group is transferred from myristoyl-CoA thioester toN-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.
