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  • Title: Cytochrome c catalyzes the in vitro synthesis of arachidonoyl glycine.
    Author: McCue JM, Driscoll WJ, Mueller GP.
    Journal: Biochem Biophys Res Commun; 2008 Jan 11; 365(2):322-7. PubMed ID: 17986381.
    Abstract:
    Long chain fatty acyl glycines are an emerging class of biologically active molecules that occur naturally and produce a wide array of physiological effects. Their biosynthetic pathway, however, remains unknown. Here we report that cytochrome c catalyzes the synthesis of N-arachidonoyl glycine (NAGly) from arachidonoyl coenzyme A and glycine in the presence of hydrogen peroxide. The identity of the NAGly product was verified by isotope labeling and mass analysis. Other heme-containing proteins, hemoglobin and myoglobin, were considerably less effective in generating arachidonoyl glycine as compared to cytochrome c. The reaction catalyzed by cytochrome c in vitro points to its potential role in the formation of NAGly and other long chain fatty acyl glycines in vivo.
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