NAD+- protein-cysteine ADP-ribosyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-cysteinyl-[protein] + NAD+ = H+ + nicotinamide + S-(ADP-D-ribosyl)-L-cysteinyl-[protein]. [PMID:25043379, RHEA:56612]

NAD+-protein-cysteine ADP-ribosyltransferase activity catalyzes the transfer of ADP-ribose from NAD+ to a cysteine residue on a target protein. This reaction involves the cleavage of the nicotinamide moiety from NAD+, leaving the ADP-ribose moiety to be attached to the cysteine residue. This process is known as ADP-ribosylation. ADP-ribosylation can have various effects on target proteins, including altering their activity, localization, and interactions with other proteins. ADP-ribosyltransferases are involved in a wide range of cellular processes, including signal transduction, DNA repair, and immune response. For example, some ADP-ribosyltransferases are involved in the regulation of cellular stress responses, while others play a role in the immune system by modifying the activity of immune cells. The activity of ADP-ribosyltransferases can be regulated by a variety of factors, including post-translational modifications, protein-protein interactions, and the availability of NAD+. Dysregulation of ADP-ribosyltransferase activity can lead to a variety of diseases, including cancer, neurodegenerative disorders, and autoimmune diseases.'
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Proteins (4)

Compounds (10)