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Adenosine diphosphate ribosyl transferase

Markowitz, M.M., Rozen, P., Pero, R.W., Tobi, M. and Miller, D.G. (1988). Hydrogen peroxide induced adenosine diphosphate ribosyl transferase (ADPRT) response in patients with inflammatory bowel disease. Gut 29, 1680-1686. [Pg.167]

Bizec JC, Mandel P, Klethi J (1985) PolyADP-ribosyl polymerase (adenosine diphosphate-ribosyl-transferase) du cristallin de bovides modulations au cours du vieillissement. C R Acad Sci 300 37-41... [Pg.9]

Honjo, J., Nishizuka, Y., Hayaishi, O., and Kato, I. (1968) Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis. J. Biol. Cbem. 243, 3553-3555. [Pg.1075]

The sirtuins (silent information regulator 2-related proteins class III HDACs) form a specific class of histone deacetylases. First, they do not share any sequence or structural homology with the other HDACs. Second, they do not require zinc for activity, but rather use the oxidized form of nicotinamide adenine dinucleotide (NAD ) as cofactor. The reaction catalyzed by these enzymes is the conversion of histones acetylated at specific lysine residues into deacetylated histones, the other products of the reaction being nicotinamide and the metabolite 2 -0-acetyl-adenosine diphosphate ribose (OAADPR) [51, 52]. As HATs and other HDACs, sirtuins not only use acetylated histones as substrates but can also deacetylate other proteins. Intriguingly, some sirtuins do not display any deacetylase activity but act as ADP-ribosyl transferases. [Pg.34]


See other pages where Adenosine diphosphate ribosyl transferase is mentioned: [Pg.300]    [Pg.300]   
See also in sourсe #XX -- [ Pg.151 ]




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