SULFATION OF PARABENS AND TYROSYLPEPTIDES BY BACTERIAL ARYLSULFATE SULFOTRANSFERASES

Authors
KIM DH KIM B KIM HS SOHNG IS KOBASHI K
Citation
Dh. Kim et al., SULFATION OF PARABENS AND TYROSYLPEPTIDES BY BACTERIAL ARYLSULFATE SULFOTRANSFERASES, Biological & pharmaceutical bulletin, 17(10), 1994, pp. 1326-1328
Citations number
14
Categorie Soggetti
Pharmacology & Pharmacy
Journal title
Biological & pharmaceutical bulletin → ACNP
ISSN journal
09186158
Volume
17
Issue
10
Year of publication
1994
Pages
1326 - 1328
Database
ISI
SICI code
0918-6158(1994)17:10<1326:SOPATB>2.0.ZU;2-7
Abstract
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.