Easy Sulphation of Phenols by a Bacterial Arylsulphotransferase
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| Publication date | 2021 |
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| Book title | Applied Biocatalysis |
| Book subtitle | The Chemist’s Enzyme Toolbox |
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| Chapter | 10.4 |
| Pages (from-to) | 381-386 |
| Publisher | Hoboken, NJ : Wiley |
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| Abstract |
The use of an enzymatic method to synthesise sulfated compounds is gaining more and more ground. The popularity is mainly due to the availability of bacterial arylsulfotransferaes (ATSs) and the convenient expression methods of the recombinant enzymes. Unlike the eukaryotic sulfotransferases, which use the very expensive 3' phosphoadenosine-5'phosphosulfate (PAPS) and are in general substrate-specific, these bacterial enzymes use cheap sulfate donors such as p-nitrophenyl sulfate (p-NPS) and N-hydroxysuccinimide sulfate. Many different compounds, including nonphenolics, have been reported to be sulfated under mild conditions. We have developed and used the recombinant AST from Desulfitobacterium hafniense, which is easily expressed in Escherichia coli. Here, we report as an example the enzymatic sulfation of E-resveratrol. Through careful selection of the concentration of the donor and the incubation time, it was possible to obtain the four different sulfated resveratrol derivatives.
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| Document type | Chapter |
| Note | Part of chapter 10: Glycosylation, Sulfation and Phosphorylation. |
| Language | English |
| Published at | https://doi.org/10.1002/9781119487043.ch10 |
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