title: Studies on the mode of action of diphtheria toxin. IV. Specificity of the cofactor (NAD) requirement for toxin action in cell-free systems.
abstract: The ability of a number of nucleotides related to NAD to replace NAD as cofactors for inhibition by diphtheria toxin of peptide bond formation has been examined. Neither NADH nor NADP are active. Of some 14 analogues closely related structurally to NAD that have been tested, only 3-thiocarboxamide pyridine-AD is as active as NAD itself. Replacement of the 3-carboxamide group on the pyridine ring by an acetyl group, or deamination of the purine ring, resulted in derivatives with reduced activity. The results were interpreted as suggesting that NAD and certain related nucleotides are capable of specific interaction with diphtheria toxin. Using the method of equilibrium dialysis, reversible binding of 1 mole of NAD per mole of toxin has been demonstrated. Toxoid does not interact with NAD.
mesh_terms: D000818:Animals; D004167:Diphtheria Toxin / Q000494:pharmacology*; D004168:Diphtheria Toxoid / Q000494:pharmacology; D006367:HeLa Cells / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D066298:In Vitro Techniques; D009243:NAD / Q000494:pharmacology*; D009711:Nucleotides / Q000494:pharmacology; D010455:Peptides / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism*; D011817:Rabbits
chemical_list: D004167:Diphtheria Toxin; D004168:Diphtheria Toxoid; D009711:Nucleotides; D010455:Peptides; D009243:NAD; D010649:Phenylalanine