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DOI: 10.1055/sos-SD-214-00162

Wever, R.; Babich, L.; Hartog, A. F.Science of Synthesis: Biocatalysis in Organic Synthesis, (20151225.

Phosphorylating enzymes belonging to the class of kinases usually carry out phosphorylation in biological systems. These enzymes use the high-energy phospho-anhydride bond in adenosine triphosphate (ATP) to transfer the phosphate moiety to alcohols to form phosphorylated esters with less energy.[‌3‌,‌4‌,‌24‌,‌25‌] To minimize the expense of ATP in synthetic procedures and also to prevent inhibition by accumulation of adenosine diphosphate (ADP), regeneration of ATP is essential. To regenerate ATP, a second kinase should be present, as should an excess (with respect to ATP) of a phosphate donor, which should be inexpensive, stable, and readily available. As discussed by Faber,[‌6‌] a number of phosphate donors and corresponding kinases have been used in regenerating systems, e.g. carbamate and carbamate kinase, creatine and creatine kinase, acetyl phosphate and acetate kinase (EC, and phosphoenol pyruvate [2-(phosphonooxy)acrylate] and pyruvate kinase (EC In these systems, the phosphoryl groups are transferred from a high-energy donor to ADP by the second kinase (Scheme 2).

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