ADP-ribosyltransferase (ART)

ADP-ribosyltransferases are a superfamily of enzymes that catalyze the transfer of ADP-ribose units from NAD^+^ to specific target proteins, nucleic acids, or other molecules[3][7]. This enzymatic activity leads to mono(ADP-ribosyl)ation or poly(ADP-ribosyl)ation, which are reversible post-translational modifications essential for controlling DNA repair, gene expression, cell proliferation, apoptosis, and responses to cellular stress[1][3][5][9]. These enzymes are widely found across different forms of life and can function as mono- or poly-ADP-ribosyl transferases. In humans, the PARP family (notably PARP1 and PARP2) are key molecular targets for anti-cancer therapies because their inhibition impairs DNA repair, making them particularly effective against tumors with deficiencies in homologous recombination repair (such as BRCA1/2 mutations)[2][4]. Members of this enzyme family are also involved in immune responses, inflammation, and can be hijacked by bacterial toxins to mediate toxicity (e.g., by cholera or diphtheria toxins)[1]. Emerging evidence links various family members to additional diseases such as neurodegeneration and cardiovascular disorders, and the family is pharmacologically targeted by several approved and investigational drugs.

Other names

ADP-ribosyltransferasePoly(ADP-ribose) polymeraseARTDMono(ADP-ribosyl)transferasePARP familyPARP1

Inhibition of DNA repair via enzymatic inhibition (PARP inhibitors block DNA repair, causing death of cancer cells with deficient repair pathways) - Induction of apoptosis through accumulation of DNA damage - Modulation of transcriptional and inflammatory pathways