NAD+-protein-C-terminal glycine ADP-ribosyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: [protein]-C-terminal glycine + NAD+ = [protein]-C-terminal O-(ADP-D-ribosyl)-glycine + nicotinamide. [PMID:28525742, RHEA:58268]

NAD+-protein-C-terminal glycine ADP-ribosyltransferase activity catalyzes the transfer of ADP-ribose from NAD+ to a protein substrate. This modification occurs specifically at the C-terminal glycine residue of the target protein. The enzyme utilizes NAD+ as a co-substrate and produces nicotinamide as a byproduct. The ADP-ribose moiety is transferred to the glycine residue, forming a covalent bond. This modification can have various effects on the target protein, including altering its activity, localization, or interaction with other proteins. The specific effects depend on the nature of the target protein and the location of the ADP-ribosylation site. This enzymatic activity is crucial for various cellular processes, including signal transduction, DNA repair, and apoptosis. It plays a role in regulating the activity of various proteins, such as transcription factors, kinases, and enzymes, by modulating their function or stability.'
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Proteins (1)

Compounds (1)