fosforyltransferaser

Fosforyltransferaser, usually referred to in English as a phosphoryl transferase or phosphotransferase, is an enzyme that catalyzes the transfer of a phosphoryl group (PO3−) from a donor molecule to an acceptor molecule. This reaction type is central to many cellular processes, including metabolism and signal transduction. Phosphoryl transferases are a diverse subset of the transferases (EC class 2) and include enzymes that move phosphate groups from donors such as ATP or phosphoenolpyruvate to various substrates.

Most commonly, these enzymes function as kinases, catalyzing the transfer of a phosphate from a nucleotide triphosphate (often ATP) to an acceptor such as a sugar, amino acid, lipid, or protein. In metabolism, examples include hexokinase (glucose to glucose-6-phosphate using ATP), phosphoglycerate kinase, and pyruvate kinase (substrate-level phosphorylation to generate ATP). In signaling, protein kinases such as serine/threonine and tyrosine kinases transfer phosphate to specific amino acid residues, modulating activity, interactions, and localization.

Mechanistic diversity exists among fosforyltransferasers. Many perform direct transfer of the terminal phosphate from the donor to the acceptor, often with Mg2+ or Mn2+ coordination to stabilize the phosphate groups. Others operate via enzyme-bound intermediates, as seen in certain two-component system histidine kinases or other specialized enzymes.

Classification and relevance: fosforyltransferasers are classified within EC 2.7 of the Enzyme Commission, encompassing phosphotransferases with a phosphate group as donor and related subcategories. They are essential for energy metabolism, growth, and regulation, and are frequent targets in biomedical research and biotechnology.