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 no.2.8.2.1
CAS no.9026-09-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Arylsulfotransferase
Identifiers
SymbolArylsulfotransferase
PfamPF05935
InterProIPR010262
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.