| 7874051 |
Kim DH, Kim B, Kim HS, Sohng IS, Kobashi K: Sulfation of parabens and tyrosylpeptides by bacterial arylsulfate sulfotransferases. Biol Pharm Bull. 1994 Oct;17(10):1326-8.
Arylsulfate sulfotransferase purified from Eubacterium A-44 has higher specific activity than the enzymes from Klebsiella K-36 and Haemophilus K-12. Propylparaben and butylparaben were good substrates among several parabens. The antibacterial activity of parabens was reduced by the sulfation of the phenolic hydroxy group. Tyrosine-containing peptides, kyotorphin, enkephalin and cholecystokinin non-sulfate, were effective as acceptor substrates by A-44, K-36 and K-12 sulfotransferases. |
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