| 摘要 |
Enzymatic sulfations of biomolecules catalyzed by 3'-phosphoadenosine-5'-phosphosulfate (PAPS) dependent sulfotransferases are enhanced by coupling the sulfation reaction an enzymatic regeneration of PAPS. The PAPS is enzymatically regenerated from its hydrolysis product 3',5'-diphosphate (PAP) using recombinant aryl sulfotransferase as the catalyst and aryl sulfate as the substrate. Biomolecules capable of enhanced sulfation by this method include carbohydrates, oligosaccharides, peptides, proteins, flavonoids, and steroids. When enzymatic sulfation and substrate regeneration steps are coupled, the desulfated aryl group produced in the regeneration step has a spectroscopic signature that can be employed for monitoring the progress of the sulfation of the biomolecule.
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