ADP Ribose Transferase is an enzyme that plays a key role in the process of post-translational modification known as ADP-ribosylation. It is responsible for the transfer of ADP-ribose moieties from nicotinamide adenine dinucleotide (NAD+) to proteins, thereby modulating their structure and function.
ADP Ribose Transferase, sometimes referred to as ART, catalyzes the transfer of ADP-ribose units from the NAD+ molecule to amino acid residues, most commonly arginine, aspartate, and glutamate. This process leads to the formation of ADP-ribose polymers or mono-ADP-ribosylated proteins, depending on the specific target and the amount of ADP-ribosylation.
The ADP-ribosylation process has been found to be involved in various cellular functions, including DNA repair, chromatin remodeling, transcriptional regulation, and signal transduction. By adding or removing ADP-ribose units, ADP Ribose Transferase can modify the activity, localization, or interactions of proteins, thus influencing their biological functions.
ADP Ribose Transferase is found in all eukaryotic organisms, including humans, and it is encoded by a family of genes known as PARP (Poly(ADP-ribose) polymerase). There are currently 17 members of the PARP family identified in humans. They differ in their substrate specificity and biological functions, but they all share the ability to transfer ADP-ribose moieties.
Overall, ADP Ribose Transferase is an essential enzyme that plays a critical role in various cellular processes by adding ADP-ribose units to proteins, thereby regulating their activity and function. Its study provides
