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An Efficient Chemoenzymatic Synthesis of Coenzyme A and Its Disulfide

Abstract : We have developed a chemoenzymatic route to coenzyme A (CoASH) and its disulfide that is amenable to gram-scale synthesis using standard laboratory equipment. By synthesizing the symmetrical disulfide of pantetheine (pantethine), we avoided the need to mask the reactive sulfhydryl and also prevented sulfur oxidation byproducts. No chromatography is required in our synthetic route to pantethine, which facilitates scale-up. Furthermore, we discovered that all three enzymes of the CoASH salvage pathway (pantetheine kinase, phosphopantetheine adenyltransferase, and dephospho-coenzyme A kinase) accept the disulfide of the natural substrates and functionalize both ends of the molecules. This yields CoA disulfide as the product of the enzymatic cascade, a much more stable form of the cofactor. Free CoASH can be prepared by in situ S–S reduction.
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Louis Mouterde, Jon Stewart. An Efficient Chemoenzymatic Synthesis of Coenzyme A and Its Disulfide. Organic Process Research and Development, American Chemical Society, 2016, 20 (5), pp.954-959. ⟨10.1021/acs.oprd.6b00059⟩. ⟨hal-02527520⟩



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