Sulfotransferase

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In biochemistry, sulfotransferases (SULTs) are transferase enzymes that catalyze the transfer of a sulfo group (R−SO3) from a donor molecule to an acceptor alcohol (R−OH) or amine (R−NH2).[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):

Sulfotransferase
Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate
Identifiers
EC no.2.8.2.-
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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]

General structure of a sulfonic acid with the blue marked functional group

Examples

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The following are examples of sulfotransferases:

See also

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References

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  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.
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