Cytochrome c catalyzes the in vitro synthesis of arachidonoyl glycine.
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.
McCue
Jeffrey M
JM
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.
Driscoll
William J
WJ
Mueller
Gregory P
GP
D000214:Acyl Coenzyme A / Q000737:chemistry*; D001095:Arachidonic Acids / Q000138:chemical synthesis*; D002384:Catalysis; D045304:Cytochromes c / Q000737:chemistry*; D004789:Enzyme Activation; D005998:Glycine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D013379:Substrate Specificity
D000214:Acyl Coenzyme A; D001095:Arachidonic Acids; C465623:N-arachidonylglycine; C026563:arachidonyl-coenzyme A; D045304:Cytochromes c; D006861:Hydrogen Peroxide; D005998:Glycine