ADP-ribosyltransferase (ART)

ADP-ribosyltransferase Overview

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.

Mechanism of Action

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

Biological Functions

Safety Considerations

Interacting Drugs

Associated Biomarkers