Beilstein J. Org. Chem.2022,18, 1278–1288, doi:10.3762/bjoc.18.134
PPK2. They are structurally unrelated and use different catalytic mechanisms. PPK1 enzymes prefer the usage of adenosine 5'-triphosphate (ATP) for polyphosphate (polyP) synthesis while PPK2 enzymes favour the reverse reaction. With the emerging use of PPK enzymes in biosynthesis, a deeper understanding
phosphate transfer potentials that are characterised by reaction yields close to full conversion, the PPK-catalysed reaction reaches an equilibrium in which about 30% ADP is left. These results were obtained for PPK1 and PPK2 enzymes, and are supported by theoretical data on the basic reaction. At high
concentrations of substrate, the different kinetic preferences of PPK1 and PPK2 can be observed. The implications of these results for the application of PPKs in chemical synthesis and as enzymes for ATP regeneration systems are discussed.
Keywords: ATP regeneration; biocatalyst; ePC-SAFT; polyp; PPK
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Graphical Abstract
Figure 1:
Polyphosphate, a ubiquitous phosphate storage molecule. Reported chain lengths range from three to ...
Beilstein J. Org. Chem.2015,11, 1713–1720, doi:10.3762/bjoc.11.186
acknowledge support from the Centre of Excellence for Biocatalysis, Biotransformations and Biocatalytic Manufacture (CoEBio3, to PPK), the FP7-PEOPLE-2011-ITN under grant agreement no. 289217 (P4fifty, to AE), the Innovative Medicines Initiative Joint Undertaking under the grant agreement no. 115360 (Chemical
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Graphical Abstract
Figure 1:
Library generation of P450cam[Tyr96Phe]-RhFRed. Active site of the P450cam-RhFRed variant Tyr96Phe ...