Sulfation pathways are an integral part of the normal metabolism of every living being. In human physiology, they are mainly implicated in bone and cartilage development and the regulation of steroid hormone action. We look at various components of sulfation pathways, among them the enzymatic apparatus for activation of the otherwise highly inert sulfate anion. So called PAPS synthases convert sulfate to active sulfate in the form of an atypical nucleotide, the cofactor PAPS that serves then for all sulfation reactions in human physiology. Recently, we could show that PAPS synthases are surprisingly fragile proteins, specifically stabilised by the nucleotide APS, an intermediate of overall PAPS biosynthesis. Together with my academic host, Professor Sabine Müller, a nucleic acid chemist from the University of Greifswald, we want to develop derivatives of PAPS and APS and test them for their ability to modulate human sulfation pathways. Such compounds will be of great value for a deeper understanding of the regulation of sex steroids by sulfation pathways and could eventually result in better treatment options of disorders of hormone excess or steroid-dependent cancers.

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