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Protein carbamoylation is a non-enzymatic post-translational modification where a carbamoyl group is covalently added to proteins, primarily at the N-terminal amino group or the ε-amino group of lysine residues. This process occurs via reaction with isocyanic acid, which can be generated from urea breakdown or through myeloperoxidase-mediated oxidation of thiocyanate during inflammation. Carbamoylation alters protein structure and function, often leading to impaired protein/enzyme activity, changes in gene expression and cell signaling, and disruption of metabolic pathways. It is associated with molecular aging and pathological conditions like chronic kidney disease and cardiovascular disease.
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