Mechanism of stimulation of ADP-ribosyltransferase in the renal brush-border membrane by EDTA.
In the presence of NAD+, renal brush-border membranes are mono-ADP-ribosylated by an endogenous ADP-ribosyltransferase. The reaction is inhibited by arginine methyl ester and is markedly stimulated by EDTA. Stimulation by EDTA is likely due, at least in part, to EDTA preventing the destruction of intact NAD+ by other enzymes in the brush-border membrane.
D036002:ADP Ribose Transferases; D000818:Animals; D004492:Edetic Acid / Q000494:pharmacology*; D006165:Guanylyl Imidodiphosphate / Q000494:pharmacology; D007672:Kidney Cortex / Q000187:drug effects / Q000648:ultrastructure*; D008871:Microvilli / Q000187:drug effects / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D009713:Nucleotidyltransferases / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases; D051381:Rats; D013696:Temperature; D013997:Time Factors
D009243:NAD; D006165:Guanylyl Imidodiphosphate; D004492:Edetic Acid; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases; D009713:Nucleotidyltransferases