- Sulfation of various alcoholic groups by an arylsulfate sulfotransferase from desulfitobacterium hafniense and synthesis of estradiol sulfate
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Bacterial arylsulfate sulfotransferases (AST) are enzymes that catalyse the transfer of a sulfate group from p-nitrophenyl sulfate (p-NPS) to a phenolic acceptor molecule. By screening of the NCBI protein database a gene coding for an AST was found in Desulfitobacterium hafniense. After expression the enzyme was purified and characterised. This AST efficiently sulfates various acceptor molecules (estrone, estradiol, enkephalin and non-phenolic alcohols) using p-NPS as sulfate donor. The purified AST has a pH optimum of 9.6, it is stable in the presence of 10% of DMSO, and depending on the conditions it has a melting temperature of up to 47°C. Surprisingly, and in great contrast to all other known bacterial ASTs, this enzyme was able to use a variety of non-phenolic alcohols as sulfate acceptor. Because of these properties, this unique enzyme is a promising tool for biotransformation processes, providing a green and simple method to specifically sulfate compounds without need for functional group protection.
- Van Der Horst, Michael A.,Van Lieshout, Johan F. T.,Bury, Aleksandra,Hartog, Aloysius F.,Wever, Ron
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supporting information
p. 3501 - 3508
(2013/02/22)
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- Use of Dimethylformamide-Sulphur Trioxide Complex as a Sulphating Agent of Tyrosine
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Dimethylformamide-sulphur trioxide (DMF-SO3) complex was found to be more suitable for tyrosine sulphation than pyridine-sulphur trioxide (Pyr-SO3) complex, the most commonly used sulphur trioxide complex for sulphation.The work-up after sulphation using
- Futaki, Shiroh,Taike, Takashi,Yagami, Takeshi,Ogawa, Toyoko,Akita, Tadashi,Kitagawa, Kouki
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p. 1739 - 1744
(2007/10/02)
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