||The enzyme, characterized from bacteria that colonize the human and mouse intestine, catalyses the transfer of a sulfate group from a phenol sulfate ester to other phenolic compounds. Activity is enhanced by Mg2+ and Mn2+ . Unlike EC 184.108.40.206, tyrosine-ester sulfotransferase and EC 220.127.116.11, aryl sulfotransferase, the enzyme does not act on 3′-phosphoadenylyl sulfate or adenosine 3′,5′-bisphosphate .
The level of sulfation of polyphenols depends on the positions of the hydroxyl groups [3-5]. Hydroxy groups of tyrosine residues in peptides such as angiotensin can also act as acceptors . The reaction proceeds according to a ping pong bi bi mechanism .
||Kim, D.-H., Konishi, L. and Kobashi, K. Purification, characterization and reaction mechanism of novel arylsulfotransferase obtained from an anaerobic bacterium of human intestine. Biochim. Biophys. Acta 872 (1986) 33–41. [PMID: 3460636]
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||Lee, N.S., Kim, B.T., Kim, D.H. and Kobashi, K. Purification and reaction mechanism of arylsulfate sulfotransferase from Haemophilus K-12, a mouse intestinal bacterium. J. Biochem. 118 (1995) 796–801. [PMID: 8576095]
||Kim, B., Hyun, Y.J., Lee, K.S., Kobashi, K. and Kim, D.H. Cloning, expression and purification of arylsulfate sulfotransferase from Eubacterium A-44. Biol. Pharm. Bull. 30 (2007) 11–14. [PMID: 17202651]