ArticleBeilstein journal of organic chemistry2022
Make or break: the thermodynamic equilibrium of polyphosphate kinase-catalysed reactions.
Article in Beilstein journal of organic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Enzymatic depolymerization of laboratory waste DNA to a dGMP-containing pool and analytical assessment of dGTP in a crude-lysate guanylate kinase system.Molecular biology reports · 2026Article
- A Universal Nucleoside-to-Nucleoside-5'-Triphosphate Enzyme Cascade Driven by Polyphosphate.Angewandte Chemie (International ed. in English) · 2026Article
- Substrate Specificity of B12-Depedent Ribonucleotide Reductases: Biotechnology and Metabolic Implications.Chembiochem : a European journal of chemical biology · 2026Article
- Identification of a distinct family of polyphosphate kinases relevant to energy homeostasis in Crenarchaeota.The Journal of biological chemistry · 2026Article
- Structure-guided engineering of a polyphosphate kinase 2 class III from anRSC chemical biology · 2025Article
- Chemo-enzymatic production of base-modified ATP analogues for polyadenylation of RNA.Chemical science · 2024Article
- Engineering the thermal stability of a polyphosphate kinase by ancestral sequence reconstruction to expand the temperature boundary for an industrially applicable ATP regeneration system.Applied and environmental microbiology · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyphosphate kinases (PPKs) have become popular biocatalysts for nucleotide 5'-triphosphate (NTP) synthesis and regeneration. Two unrelated families are described: PPK1 and 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 of the enzymes and their thermodynamic reaction course is of need, especially in comparison to other kinases. Here, we tested four PPKs from different organisms under the same conditions without any coupling reactions. In comparison to other kinases using phosphate donors with comparably higher 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.
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