Sulfation of parabens and tyrosylpeptides by bacterial arylsulfate sulfotransferases |
| |
Authors: | DH Kim B Kim HS Kim IS Sohng K Kobashi |
| |
Affiliation: | College of Pharmacy, Kyung-Hee University, Seoul, Korea. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|