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Nitric oxide and NAD-dependent protein modification

  • Part VI: Derivation of Proteins with ADP-ribose, NAD and their Analogues
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Abstract

Nitric oxide (NO) has been suggested to act as a regulator of endogenous intracellular ADP-ribosylation, based on radiolabelling of proteins in tissue homogenates incubated with [32P]NAD and No. After the NO-stimulated modification was replicated in a defined system containing only the purified acceptor protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the hypothesis of NO-stimulation of an endogenous ADP-ribosyltransferase became moot. The NO-stimulated, NAD-dependent modification of GAPDH was recently characterized as covalent binding of the whole NAD molecule to the enzyme, not ADP-ribosylation. With this result, along with the knowledge that GAPDH is stoichiometrically S-nitrosylated, the role of NO in protein modification with NAD may be viewed as the conferring of an unexpected chemical reactivity upon GAPDH, possibly due to nitrosylation of a cysteine in the enzyme active site.

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Authors and Affiliations

  1. Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 10/ 5N-307, 20892, Bethesda, MD, USA

    Lee J. McDonald & Joel Moss

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  1. Lee J. McDonald
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  2. Joel Moss
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McDonald, L.J., Moss, J. Nitric oxide and NAD-dependent protein modification. Mol Cell Biochem 138, 201–206 (1994). https://doi.org/10.1007/BF00928462

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