adenylylatemediated

Adenylylation is a post-translational modification where an adenylyl group (an adenosine monophosphate moiety) is covalently attached to a protein. This process is catalyzed by adenylyltransferases, which transfer the adenylyl group from ATP to a target amino acid residue on the protein. The specific amino acid residue that can be adenylylated varies depending on the enzyme and the substrate protein, but common targets include tyrosine, serine, and threonine. Adenylylation can significantly alter the function, activity, localization, or stability of the modified protein. It is a reversible process, with deadenylylases capable of removing the adenylyl group, allowing for dynamic regulation of protein function. This modification plays a crucial role in various cellular processes, including signal transduction, enzyme regulation, and metabolic pathways. For example, adenylylation is involved in the regulation of bacterial enzyme activity and in the modification of glutamine synthetase in bacteria, which impacts nitrogen metabolism. The precise mechanisms and biological significance of adenylylation are still areas of active research, with new adenylylated proteins and regulatory roles being discovered.