Sulfotransferase

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 sulfamate (R-NH-SO3). Both reactive groups for a sulfonation via sulfotransferases may be part of a protein, lipid, carbohydrate or steroid.[2]

Examples

Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate

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.
  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.

External links

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