NAD Arginine ADP Ribosyltransferase, also known as NAD+-dependent ADP ribosyltransferase, is an enzyme involved in the post-translational modification of proteins. It catalyzes the transfer of an ADP-ribose group from nicotinamide adenine dinucleotide (NAD+) to specific arginine residues on target proteins.
This enzyme plays a crucial role in various cellular processes, including regulating protein function, molecular signaling, DNA repair, and immune response. Through the process of ADP-ribosylation, NAD Arginine ADP Ribosyltransferase can modify the activity, stability, and subcellular localization of target proteins, thus influencing their function within the cell.
ADP-ribosylation is a reversible modification that can alter protein-protein interactions, enzymatic activities, and DNA binding capacities. It can also act as a signaling event, affecting cellular processes such as gene expression, cell cycle progression, and apoptosis. NAD Arginine ADP Ribosyltransferase is involved in mediating these ADP-ribosylation reactions by specifically recognizing and modifying specific arginine residues on target proteins.
The enzymatic activity of NAD Arginine ADP Ribosyltransferase is dependent on the availability of NAD+ as a substrate, which is cleaved to release ADP-ribose during the ADP-ribosylation process. This enzyme is highly conserved across species and is found in a wide range of organisms, including bacteria, plants, and animals.
Overall, NAD Arginine ADP Ribosyltransferase plays a critical role in regulating protein function and molecular signaling pathways, contributing to the proper functioning and maintenance of various cellular processes.
