Dh. Kim et al., SULFATION OF PARABENS AND TYROSYLPEPTIDES BY BACTERIAL ARYLSULFATE SULFOTRANSFERASES, Biological & pharmaceutical bulletin, 17(10), 1994, pp. 1326-1328
Arylsulfate sulfotransferase purified from Eubacterium A-44 has higher
specific activity than the enzymes from Klebsiella K-36 and Haemophil
us K-12. Propylparaben and butylparaben were good substrates among sev
eral parabens. The antibacterial activity of parabens was reduced by t
he sulfation of the phenolic hydroxy group. Tyrosine-containing peptid
es, kyotorphin, enkephalin and cholecystokinin non-sulfate, were effec
tive as acceptor substrates by A-44, K-36 and K-12 sulfotransferases.