The inactivation of bovine heart glyceraldehyde-3-phosphate dehydrogenase by phosphatidylinositol (PI) and phosphatidylserine (PS) in the form of liposomes was investigated in the presence and absence of NAD excess. In the absence of NAD, the enzyme activity decreased to about ~0% of its initial value at 0.6 mM PI and 0.8 mM PS (lipid-to-protein molar ratio 600 and 800, respectively). In the same lipid concentration range almost full regainment of the activity was observed in the presence of 80/~M NAD. It was shown that the excess of NAD protects the enzyme against conformational change induced by the phospholipids. Centrifugation experiments showed that both PI and PS bind significant amounts of NAD.Glyceraldehyde-3-phosphate dehydrogenase; Phosphatidylinositol; Phosphatidylserine; Lipid-protein interaction
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.