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Sulfation of Various Alcoholic Groups by an Arylsulfate Sulfotransferase from Desulfitobacterium hafniense and Synthesis of Estradiol Sulfate
Author(s) -
van der Horst Michael A.,
van Lieshout Johan F. T.,
Bury Aleksandra,
Hartog Aloysius F.,
Wever Ron
Publication year - 2012
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201200564
Subject(s) - chemistry , sulfation , sulfate , acceptor , enzyme , sulfotransferase , biotransformation , sulfatase , biochemistry , organic chemistry , stereochemistry , physics , condensed matter physics
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.