ArticleNature communications2026
A universal polyphosphate kinase powers in vitro transcription.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- A Modular Nucleoside Kinase Cascade for the Synthesis of Ribonucleoside Triphosphates.Biotechnology and bioengineering · 2026Article
- A Universal Nucleoside-to-Nucleoside-5'-Triphosphate Enzyme Cascade Driven by Polyphosphate.Angewandte Chemie (International ed. in English) · 2026Article
- Polyphosphate Attenuates Oxidative Stress to Support Temperature Adaptability in Hot Spring Cyanobacteria.Plants (Basel, Switzerland) · 2026Article
- Structure-guided engineering of a polyphosphate kinase 2 class III from anRSC chemical biology · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Polyphosphate kinases (PPKs) catalyze phosphoryl transfer between polyphosphates and nucleotides. Polyphosphates are a cost-effective source of phosphorylating power, making PPKs attractive enzymes for nucleotide production. However, at present, applications that require the simultaneous utilization of diverse nucleotides are not possible due to the restricted substrate profiles of PPKs. Here, we present a universal PPK capable of efficiently phosphorylating all eight common ribonucleotides (purines and pyrimidines, monophosphates and diphosphates) to triphosphates. Under optimal conditions, ~70% triphosphate conversion was observed for each substrate. To demonstrate the biotechnological potential of a universal PPK, we developed a one-pot assay for PPK-powered in vitro transcription. Primitive biology likely relied on enzyme promiscuity to support nascent metabolism with a compact proteome. This work highlights how applying the same principle to synthetic biology can facilitate the construction of complex in vitro reaction systems.
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Registered trials
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