Affiliation:
1. Department of Biochemical and Chemical Engineering TU Dortmund University Emil-Figge-Straße 66 44227 Dortmund Germany
2. Department of Chemistry Johannes Gutenberg University Mainz Duesbergweg 10–14 55128 Mainz Germany
3. School of Science Constructor University Campus Ring 6 28759 Bremen Germany
Abstract
AbstractAdenosine‐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 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.
Subject
Electrochemistry,Catalysis