ArticleProceedings of the National Academy of Sciences of the United States of America2018
Substrate recognition and mechanism revealed by ligand-bound polyphosphate kinase 2 structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 73 citations in OpenAlex.
- Two-step bioconversion of pyridoxal 5'-phosphate from pyridoxine through cofactor regeneration and pyridoxine 5'-phosphate oxidase evolution.Synthetic and systems biotechnology · 2026Article
- Identification of a distinct family of polyphosphate kinases relevant to energy homeostasis in Crenarchaeota.The Journal of biological chemistry · 2026Article
- A universal polyphosphate kinase powers in vitro transcription.Nature communications · 2026Article
- Structure-guided engineering of a polyphosphate kinase 2 class III from anRSC chemical biology · 2025Article
- Polyphosphate Kinase fromInternational journal of molecular sciences · 2024Article
- Fluoride and gallein regulate polyphosphate accumulation in dental caries-associatedMicrobiology (Reading, England) · 2024Article
- Chemo-enzymatic production of base-modified ATP analogues for polyadenylation of RNA.Chemical science · 2024Article
- Dissolved organic phosphorus bond-class utilization by Synechococcus.FEMS microbiology ecology · 2024Article
- Engineering sulfonate group donor regeneration systems to boost biosynthesis of sulfated compounds.Nature communications · 2023Article
- Efficient synthesis of Ala-Tyr by L-amino acid ligase coupled with ATP regeneration system.Applied biochemistry and biotechnology · 2023Article
- Multi-enzyme catalysed processes using purified and whole-cell biocatalysts towards a 1,3,4-substituted tetrahydroisoquinoline.RSC advances · 2023Article
- Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases.Environmental science & technology · 2022Article
- Synthetic metabolism forRSC chemical biology · 2022Article
- Beyond Triphosphates: Reagents and Methods for Chemical Oligophosphorylation.Journal of the American Chemical Society · 2022Review
- Dissolved organic phosphorus utilization by the marine bacterium Ruegeria pomeroyi DSS-3 reveals chain length-dependent polyphosphate degradation.Environmental microbiology · 2022Article
- Polyphosphate Kinase 2 (PPK2) Enzymes: Structure, Function, and Roles in Bacterial Physiology and Virulence.International journal of molecular sciences · 2022Review
- Make or break: the thermodynamic equilibrium of polyphosphate kinase-catalysed reactions.Beilstein journal of organic chemistry · 2022Article
- In vitro biosynthesis of ATP from adenosine and polyphosphate.Bioresources and bioprocessing · 2021Article
- Article
- Production of the Carboxylate Reductase from Nocardia otitidiscaviarum in a Soluble, Active Form for in vitro Applications.Chembiochem : a European journal of chemical biology · 2021Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inorganic polyphosphate is a ubiquitous, linear biopolymer built of up to thousands of phosphate residues that are linked by energy-rich phosphoanhydride bonds. Polyphosphate kinases of the family 2 (PPK2) use polyphosphate to catalyze the reversible phosphorylation of nucleotide phosphates and are highly relevant as targets for new pharmaceutical compounds and as biocatalysts for cofactor regeneration. PPK2s can be classified based on their preference for nucleoside mono- or diphosphates or both. The detailed mechanism of PPK2s and the molecular basis for their substrate preference is unclear, which is mainly due to the lack of high-resolution structures with substrates or substrate analogs. Here, we report the structural analysis and comparison of a class I PPK2 (ADP-phosphorylating) and a class III PPK2 (AMP- and ADP-phosphorylating), both complexed with polyphosphate and/or nucleotide substrates. Together with complementary biochemical analyses, these define the molecular basis of nucleotide specificity and are consistent with a Mg
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.