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Sulfotransferase

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The structure and bonding of the sulfate ion

Sulfotransferases EC 2.8.2. are transferase enzymes that catalyze the transfer of a sulfo group (not a sulfate group) from a donor molecule to an acceptor alcohol or amine.[1] The most common sulfo group donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In the case of alcohol as acceptor, the product is a sulfate (R-OSO3-), whereas an amine leads to a sulfo-amine (R-NH-SO3-). Both reactive groups for a sulfonation via sulfotransferases may be part of a protein, lipid, carbohydrate or steroid.[2]

Examples

The following are examples of sulfotransferases:

See also

References

  1. ^ Negishi M; Pedersen LG; Petrotchenko E; et al. (2001). "Structure and function of sulfotransferases". Arch. Biochem. Biophys. 390 (2): 149–57. doi:10.1006/abbi.2001.2368. PMID 11396917. {{cite journal}}: Unknown parameter |author-separator= ignored (help)
  2. ^ Rath VL, Verdugo D, Hemmerich S (2004). "Sulfotransferase structural biology and inhibitor discovery". Drug Discov. Today. 9 (23): 1003–11. doi:10.1016/S1359-6446(04)03273-8. PMID 15574316.{{cite journal}}: CS1 maint: multiple names: authors list (link)