Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Arylsulfotransferase / chemistry
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Arylsulfotransferase / isolation & purification
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Arylsulfotransferase / metabolism*
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Cholecystokinin / metabolism
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Endorphins / metabolism
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Enkephalin, Leucine / metabolism
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Eubacterium / enzymology*
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Feces / enzymology
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Feces / microbiology
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Fungi / drug effects
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Haemophilus / enzymology
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Humans
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Hydrogen-Ion Concentration
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Hydroxybenzoates / metabolism
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Intestines / enzymology
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Intestines / microbiology
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Klebsiella / enzymology
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Male
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Mice
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Naphthols / metabolism
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Parabens / chemistry
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Parabens / metabolism*
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Parabens / pharmacology
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Phenols / metabolism
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Rats
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Staphylococcus aureus / drug effects
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Substrate Specificity
Substances
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Endorphins
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Hydroxybenzoates
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Naphthols
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Parabens
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Phenols
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kyotorphin
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1-naphthol
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butylparaben
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Enkephalin, Leucine
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Cholecystokinin
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Arylsulfotransferase
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arylsulfate sulfotransferase
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propylparaben