Cytochrome c catalyzes the in vitro synthesis of arachidonoyl glycine |
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Authors: | McCue Jeffrey M Driscoll William J Mueller Gregory P |
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Affiliation: | Department of Anatomy Physiology and Genetics, Uniformed Services University of the Health Sciences, F. Edward Herbert School of Medicine, 4301 Jones Bridge Road, Bethesda, MD 20814, USA |
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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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Keywords: | Arachidonoyl glycine Cytochrome c Long chain fatty acyl glycine Arachidonoyl CoA Glycine Hydrogen peroxide |
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