Abstract
Sulfation is a common modification of extracelluar glycans and tyrosine residues on proteins, which is important in many signalling pathways and interactions. Existing methods for studying sulfotransferases, the enzymes that catalyse sulfation, are cumbersome and low-throughput. Recent studies published in the Biochemical Journal have repurposed established biochemical assays from the kinase field and applied them to the characterisation of sulfotransferases. Biochemical screening of a library of kinase inhibitors revealed that compounds that target RAF kinases may also be repurposed to inhibit sulfotransferases. Together with the available structures of sulfotransferases, these studies open the door to the development of chemical tools to probe the biological functions of these important enzymes.
Highlights
Biological sulfation is a widespread covalent chemical modification of biomolecules by the addition of a sulfonyl group (SOÀ3 ) [1]
Whereas protein kinases use ATP as a source of bioavailable phosphate to phosphorylate their target proteins, inorganic sulfate is made available for incorporation into biomolecules in the form of PAPS (30-phosphoadenosine 50-phosphosulfate) through a process in which ATP is first sulfated by the ATP sulfurylase enzyme to generate adenosine 50-phosphosulfate, which is phosphorylated on the 30 position of the ribose ring to generate
A subset of HS6ST1 mutations that are implicated in idiopathic hypogonadotrophic hypogonadism (IHH), a genetic disease characterised by delayed onset of puberty, map to the catalytic domain of the enzyme and may contribute to the recognition of glycan substrate [8]
Summary
Biological sulfation ( called sulfonation) is a widespread covalent chemical modification of biomolecules by the addition of a sulfonyl group (SOÀ3 ) [1]. Sulfated glycans fulfil important biological functions in the extracellular matrix and on the surfaces of cells, providing structural strength and mediating signalling via specific binding interactions, and the process of sulfation is carefully regulated within the Golgi network.
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