NADP Arginine ADP Ribosyltransferase, also known as NADP-arginine mono-ADP-ribosyltransferase or NADP-ADP-ribosyltransferase, is an enzyme involved in post-translational modifications of proteins. It is a specific type of ADP-ribosyltransferase that catalyzes the transfer of ADP-ribose moieties from nicotinamide adenine dinucleotide phosphate (NADP) to arginine residues in target proteins. This modification is termed ADP-ribosylation and is a reversible process that plays important roles in various cellular functions.
The enzyme NADP Arginine ADP Ribosyltransferase is responsible for adding the ADP-ribose group to the target protein, which can alter its structure, function, or binding affinity. This modification can affect diverse cellular processes such as DNA repair, signal transduction, metabolism, and gene expression regulation. Moreover, it has also been implicated in the defense mechanisms against bacterial toxins and pathogens.
The NADP Arginine ADP Ribosyltransferase enzyme has a highly specific recognition pattern for target proteins and arginine residues, which determines its substrate specificity. This enzyme is often found in various organisms, including bacteria, plants, and animals, indicating its evolutionary conservation and functional significance.
The study of NADP Arginine ADP Ribosyltransferase and its target proteins has gained much attention in the field of biochemistry and molecular biology due to its involvement in multiple signaling pathways and disease-related processes, like cancer, neurodegeneration, and autoimmune disorders. Understanding the mechanism and regulation of this enzyme can provide valuable insights into cellular processes and potentially pave the way for therapeutic interventions targeting ADP-rib
