Photochemical Transfer of the Nicotinamide Moiety of NAD to a Specific Residue in the Catalytic Center of Diphtheria Toxin Fragment A

Autor:	Pamela F. Crain, James A. McCloskey, S F Carroll, R. John Collier, Norman J. Oppenheimer, Thomas M. Marschner
Rok vydání:	1985
Předmět:	chemistry.chemical_classification Diphtheria toxin biology Nicotinamide Chemistry Stereochemistry Active site Photochemistry Elongation factor chemistry.chemical_compound Enzyme biology.protein Moiety Pseudomonas exotoxin NAD+ kinase
Zdroj:	Proceedings in Life Sciences ISBN: 9783642705915
DOI:	10.1007/978-3-642-70589-2_77
Popis:	Photolabeling with enzyme substrates, effectors, or photolabile analogs thereof is one of the most useful means of identifying active site residues within the primary structures of enzymes. We have recently applied this method to the study of the NAD-binding sites of two mono(ADP-ribosyl) transferases, diphtheria toxin (DT) and exotoxin A (PT) from Pseudomonas aeruginosa. Both toxins (after appropriate activation steps) transfer ADP-ribose from NAD to elongation factor 2, and as a side reaction, catalyze the hydrolysis of NAD to ADP-ribose, nicotinamide, and a proton.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1110875b7e742048cf823e09d28e63dd https://doi.org/10.1007/978-3-642-70589-2_77 Zobrazit plný text záznamu