Comparison of the acyl chain specificities of human myristoyl-CoA synthetase and human myristoyl-CoA:protein N-myristoyltransferase was written by Kishore, Nandini S.;Wood, David C.;Mehta, Pramod P.;Wade, Arlene C.;Lu, Tianbao;Gokel, George W.;Gordon, Jeffrey I.. And the article was included in Journal of Biological Chemistry in 1993.Reference of 3903-40-0 This article mentions the following:
Myristoyl-CoA synthetase (I) and protein N-myristoyltransferase (II) were partially purified from a human erythroleukemia cell line. Their substrate specificities were examined using 2 in vitro assays of enzyme activity together with a panel of C7-C17 saturated fatty acids plus 72 myristic acid analogs containing O, S, ketocarbonyl, ester, amide, cis and trans double bonds, triple bonds, and para-substituted Ph groups. There was an inverse relation between the polarity and the activity of C14 fatty acid substrates of I. Surveys of tetradecenoic and tetradecynoic acids suggested that myristate is bound to I in a bent conformation with a principal bend occurring in the vicinity of C5-C6. I was able to tolerate a somewhat wider range of physicochem. properties in acyl chains than was the monomeric human II. However, like I, there was an inverse relation between acyl chain polarity and the activities of the acyl-CoA substrates of II. Moreover, the acyl chain of myristoyl-CoA appeared to be bound to II in a bent conformation with bends located in the vicinity of C5 and C8. The acyl chain specificities of both enzymes make them well suited to utilize efficiently any cellular pools of 5Z-tetradecenoic and 5Z,8Z-tetradecadienoic acids and their CoA derivatives This feature may account for the recent observation that in some mammalian cell lineages, certain N-myristoyl-proteins are heterogeneously acylated with these C14 fatty acids. Finally, the acyl-CoA binding sites of human and Saccharomyces cerevisiae II appeared to have been highly conserved. Given their overlapping yet distinct peptide substrate specificities, the development of species-specific inhibitors of II should probably focus on structural features recognized in the enzyme peptide substrates rather than in the acyl chain of their acyl-CoA substrates. In the experiment, the researchers used many compounds, for example, 12-Methoxy-12-oxododecanoic acid (cas: 3903-40-0Reference of 3903-40-0).
12-Methoxy-12-oxododecanoic acid (cas: 3903-40-0) belongs to esters. Esters are also usually derived from carboxylic acids. It may also be obtained by reaction of acid anhydride or acid halides with alcohols or by the reaction of salts of carboxylic acids with alkyl halides. Esters contain a carbonyl center, which gives rise to 120° C–C–O and O–C–O angles. Unlike amides, esters are structurally flexible functional groups because rotation about the C–O–C bonds has a low barrier. Their flexibility and low polarity is manifested in their physical properties; they tend to be less rigid (lower melting point) and more volatile (lower boiling point) than the corresponding amides. Reference of 3903-40-0
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