Aryl sulfotransferase

An aryl sulfotransferase (EC 2.8.2.1) is an enzyme that transfers a sulfate group from phenolic sulfate esters to a phenolic acceptor substrate.[1]

3'-phosphoadenylyl sulfate + a phenol adenosine 3',5'-bisphosphate + an aryl sulfate
aryl sulfotransferase
Identifiers
EC number2.8.2.1
CAS number9026-09-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Arylsulfotransferase
Identifiers
SymbolArylsulfotransferase
PfamPF05935
InterProIPR010262

Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and phenol, whereas its two products are adenosine 3',5'-bisphosphate and aryl sulfate.

These enzymes are transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:phenol sulfotransferase. Other names in common use include phenol sulfotransferase, sulfokinase, 1-naphthol phenol sulfotransferase, 2-naphtholsulfotransferase, 4-nitrocatechol sulfokinase, arylsulfotransferase, dopamine sulfotransferase, p-nitrophenol sulfotransferase, phenol sulfokinase, ritodrine sulfotransferase, and PST. This enzyme participates in sulfur metabolism.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1LS6, 1Z28, 1Z29, 2A3R, and 2D06.

References

  1. Kim SK, Baek MC, Kim DH, Kim BK, Choi EC (1996). "Cloning and sequencing of the Klebsiella K-36 astA gene, encoding an arylsulfate sulfotransferase". Microbiol. Immunol. 40 (8): 531–537. doi:10.1111/j.1348-0421.1996.tb01105.x. PMID 8887346.

Further reading

  • Romain Y, Demassieux S, Carriere S (1982). "Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines". Biochem. Biophys. Res. Commun. 106 (3): 999–1005. doi:10.1016/0006-291X(82)91810-1. PMID 6956338.
  • Sekura RD, Jakoby WB (1979). "Phenol sulfotransferases". J. Biol. Chem. 254 (13): 5658–63. PMID 447677.


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