Sulfotransferases

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Sulfotransferases
Enzyme classification
EC, category 2.8.2. ,  Transferase
Response type Transfer of sulfate groups

Sulfotransferases ( EC  2.8.2.- ) are enzymes which sulfo groups transmitted. They occur in eubacteria and eukaryotes and are divided into membrane-associated and soluble sulfotransferases.

reaction

Sulfotransferases transfer the sulfo group from the cosubstrate 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to acceptor groups such as hydroxyl groups or amines of various substrates . This creates 3'-phosphoadenosine-5'-phosphate (PAP). Since alcohols (R-OH) are often sulfonated as substrates by sulfotransferases and thus sulfate esters (R-OSO 3 - ) are formed as products , one often speaks of sulfation , but biochemically incorrectly .

In addition to oxygen functions, z. B. also nitrogen functions are sulfonated: Aniline (Ar-NH 2 ) is sulfonated by sulfotransferases, whereby the sulfonamine of aniline (Ar-NH-SO 3 - ) is formed as the product and not a sulfate. In animals, the enzymes act as homodimers and heterodimers , in plants as monomers .

Occurrence and function

Due to their occurrence in the cell, the sulfotransferases are divided into two groups. Group 1 consists of membrane-associated sulfotransferases, the macromolecules such. B. Accept proteins and glycosaminoglycans . Enzymes of this group have been found in animals and plants. Members of the second group are soluble sulfotransferases, they accept small organic molecules such as flavonoids , steroids , neurotransmitters and xenobiotics . Members of the second group are again divided into two subgroups based on their function. Enzymes of the first subgroup have a function in detoxification , those of the second subgroup are involved in metabolic processes such as e.g. B. involved in the inactivation of steroids. The first group uses a wide range of substrates, while the second group is highly specific for its substrate.

Individual evidence

  1. ↑ a b M Negishi, LG Pedersen, E Petrotchenko, S Shevtsov, A Gorokhov, Y Kakuta, LC Pedersen: Structure and function of sulfotransferases . In: Arch Biochem Biophys 390, 2001, 149-157.
  2. ↑ a b RM Weinshilboum, DM Otterness, IA Aksoy, TC Wood, C Her, RB Raftogianis: Sulfotransferase molecular biology: cDNAs and genes . FASEB J . 11, 1997, 3-14.
  3. ↑ L Varin, RK Ibrahim: Partial purification and characterization of three flavonol-specific sulfotransferases from Flaveria chloraefolia . In: Plant Physiol. 90, 1989, 977-981.
  4. ^ C Niehrs, R Beisswanger, Wieland B. Huttner : Protein tyrosine sulfation , 1993 - an update. Chem. Biol. Interact. 92, 1994, 257-271.
  5. ^ KG Bowman, CR Bertozzi : Carbohydrate sulfotransferases: Mediators of extracellular communication . Chem. Biol. 6, 1999, R9-R22.
  6. ↑ O Habuchi: Diversity and functions of glycosaminoglycan sulfotransferases . Biochim. Biophys. Acta 1474, 2000, 115-127.
  7. ↑ H Hanai, D Nakayama, HP Yang, Y Matsubayashi, Y Hirota, Y Sakagami: Existence of a plant tyrosylprotein sulfotransferase: novel plant enzyme catalyzing tyrosine O-sulfation of preprophytosulfokine variants in vitro . FEBS Lett . 470, 2000, 97-101.
  8. ↑ L Varin, V DeLuca, RK Ibrahim, N Brisson: Molecular characterization of two plant flavonol sulfotransferases . Proc. Natl. Acad. Sci. USA 89, 1992, 1286-1290
  9. ↑ RM Weinshilboum, DM Otterness: sulfotransferase enzyme . In: FC Kauffman (ed.): Handbook of Experimental Pharmacology , Springer, Berlin 1994, 45-78.
  10. ↑ M Rouleau, F Marsolais, M Richard, L Nicolle, B Voigt, G Adam L Varin: Inactivation of brassinosteroid biological activity by a salicylate-inducible steroid sulfotransferase from Brassica napus . J. Biol. Chem. 274, 1999, 20925-20930.
  11. ↑ F Marsolais, SK Gidda, J Boyd, L Varin: Plant soluble sulfotransferases: Structural and functional similarity with mammalian enzymes . Recent Advances in Phytochem. 34, 2000, 433-456.