fosforylacj

Fosforylacj, known in English as phosphorylation, is a biochemical process in which a phosphate group is covalently attached to an organic molecule. The phosphate is typically donated by ATP and transferred to the substrate by enzymes called kinases. The reaction is generally reversible through the action of phosphatases, which remove the phosphate group.

In biology, phosphorylation is a widespread mechanism for regulating the function of proteins and other biomolecules. In most eukaryotes, protein phosphorylation occurs mainly on serine, threonine, or tyrosine residues, altering enzyme activity, interactions, localization, or stability. In bacteria and some archaea, phosphorylation often involves histidine residues in two-component signaling systems that control responses to environmental changes. Phosphorylation can also modify lipids and carbohydrates, affecting membrane properties and metabolic flux.

Phosphorylation plays central roles in numerous cellular processes, including metabolism, signal transduction, gene expression, and cell division. It is a dynamic and tightly controlled modification, governed by the balance between kinases and phosphatases in cells. Dysregulation of phosphorylation pathways is linked to a range of diseases, notably cancer, metabolic disorders, and neurodegenerative conditions.

Detection and study of phosphorylation rely on methods such as mass spectrometry and phospho-specific antibodies, which reveal the sites and patterns of phosphorylation. These approaches help researchers understand how signaling networks respond to stimuli and how perturbations in phosphorylation contribute to disease.