Sulfotransferasen

Sulfotransferasen, or sulfotransferases, are a family of enzymes that catalyze the transfer of a sulfate group from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to acceptor molecules. This reaction yields a sulfated product and 3'-phosphoadenosine-5'-phosphate (PAP). Sulfation modifies the chemical and biological properties of substrates, influencing their solubility, activity, transport, and interactions.

In humans, sulfotransferases are organized into several families with distinct cellular localizations and substrate scopes. Cytosolic sulfotransferases (SULTs) are soluble enzymes mainly found in liver, intestine, kidney, and brain. Key members include SULT1A1, SULT1A2, SULT1A3, SULT1E1, and SULT2A1, among others. These enzymes typically sulfate small molecules such as phenols, catecholamines, and steroids, playing important roles in drug metabolism, hormone regulation, and detoxification. Genetic polymorphisms in SULT genes can affect sulfation capacity and influence drug response and disease susceptibility.

Tyrosylprotein sulfotransferases (TPST1 and TPST2) are Golgi-resident enzymes that sulfate tyrosine residues on secreted and membrane proteins, modifying protein function and signaling.

Carbohydrate sulfotransferases (CHST family) in the Golgi add sulfate to glycosaminoglycans and other carbohydrate structures, shaping tissue-specific sulfation patterns.

Clinical and physiological relevance stems from modulation of drug efficacy and toxicity, hormone homeostasis, and the regulation of cellular signaling. Regulation occurs at transcriptional and post-translational levels and is influenced by genetics, development, and disease state.