  Adenosine-5'-triphosphate (ATP) plays a crucial role in many biocatalytic
reactions and its regeneration can influence the performance of a related
enzymatic reaction significantly. Here, we established an electrochemically
coupled ATP regeneration by pyruvate oxidase and acetate kinase (ACK) for the
phosphorylation of mevalonate catalyzed by mevalonate kinase. A yield of 84%
for the product mevalonate phosphate was reached and a total turnover number
for ADP of 68. These metrics are promising for the development of an economic
feasible bioprocess and surpass many other enzymatic ATP regeneration systems.
A comparison was made to polyphosphate kinases (PPKs), ACK, pyruvate kinase,
and creatine kinase in terms of the phosphate donor properties and biocatalytic
metrics of exemplary reactions. Furthermore, our system was expanded by a PPK
that enables the phosphorylation of AMP, which can broaden the spectrum of
applications even further.
