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- W1984702997 abstract "An ADP-ribosyltransferase was found in elongation factor 2 (EF-2) preparations from polyoma virus-transformed baby hamster kidney (pyBHK) cells. Like fragment A of diphtheria toxin and Pseudomonas toxin A, this eukaryotic cellular enzyme transfers [14C]adenosine from NAD+ to EF-2. However, the cellular transferase is immunologically distinct from fragment A. The transferase also can be distinguished from fragment A and Pseudomonas toxin A by the inhibition of the activity of the former by cytoplasmic extracts and by histamine. Snake venom phosphodiesterase digestion of the [14C]adenosine-labeled EF-2 product of the cellular transferase reaction yielded [14C]AMP, indicating that the cellular enzyme is a mono(ADP-ribosyl)transferase. The forward ADP-ribosylation reaction catalyzed by the cellular enzyme is reversed by fragment A, yielding [14C]NAD+. The results strongly suggest that the cellular transferase is a mono(ADP-ribosyl)transferase, which ADP-ribosylates the same diphthamide residue of EF-2 as does fragment A and Pseudomonas toxin A." @default.
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- W1984702997 date "1984-05-01" @default.
- W1984702997 modified "2023-09-23" @default.
- W1984702997 title "Cellular ADP-ribosyltransferase with the same mechanism of action as diphtheria toxin and Pseudomonas toxin A." @default.
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- W1984702997 doi "https://doi.org/10.1073/pnas.81.9.2703" @default.
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