Transferases are a major class of Enzymes that catalyze the transfer of a specific functional group from a donor molecule to an acceptor, constituting one of the principal categories in the standard enzyme classification system. The groups transferred define their subclasses and include phosphate groups, moved by ki…
Transferases are a major class of Enzymes that catalyze the transfer of a specific functional group from a donor molecule to an acceptor, constituting one of the principal categories in the standard enzyme classification system. The groups transferred define their subclasses and include phosphate groups, moved by kinases and phosphotransferases; methyl and other one-carbon units, by methyltransferases; acyl, glycosyl, and amino groups; and sulfur- and nitrogenous-containing moieties. Through these reactions transferases are central to intermediary metabolism, governing the processing of carbohydrates, lipids, proteins, and nucleic acids, and to regulatory mechanisms such as signal transduction and post-translational modification. Glycosyltransferases, for example, build and remodel polysaccharides, and their activity is studied through dedicated assay methods, while serum transferase activity serves as a biomarker of tissue, particularly hepatic and muscular, injury, as illustrated by altered enzyme levels following toxicant exposure in liver and muscle. Several transferases intersect with redox biology and free-radical handling, linking the class to oxidative metabolism. Because their precise group-transfer chemistry maintains metabolic balance, disturbances in transferase activity through inhibition, mutation, or induction have physiological and pathological consequences. Research addresses the catalytic mechanisms and assay of transferases, their roles in metabolism and macromolecule biosynthesis, and their use as biomarkers of organ injury.
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