ArticleActa crystallographica. Section F, Structural biology communications2018
Crystal structure of Escherichia coli purine nucleoside phosphorylase in complex with 7-deazahypoxanthine.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Exploring Novel Indazole and Pyrazole Nucleoside Analogues: Enzymatic Synthesis, Characterization, and Biological Evaluation.International journal of molecular sciences · 2026Article
- Untargeted Metabolomics Reveals Metabolic Reprogramming During Viable but Non-Culturable State Formation inFoods (Basel, Switzerland) · 2026Article
- The impact of rumen and hindgut microbiomes on the persistent productivity of long-lived dairy cows.Microbiome · 2026Article
- Enzymatic Transglycosylation Features in Synthesis of 8-Aza-7-Deazapurine Fleximer Nucleosides by RecombinantBiomolecules · 2024Article
- Design and Synthesis of New Modified Flexible Purine Bases as Potential Inhibitors of Human PNP.Molecules (Basel, Switzerland) · 2023Article
- Synthesis of New 5'-Norcarbocyclic Aza/Deaza Purine Fleximers - Noncompetitive Inhibitors ofFrontiers in chemistry · 2022Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purine nucleoside phosphorylases (EC 2.4.2.1; PNPs) reversibly catalyze the phosphorolytic cleavage of glycosidic bonds in purine nucleosides to generate ribose 1-phosphate and a free purine base, and are key enzymes in the salvage pathway of purine biosynthesis. They also catalyze the transfer of pentosyl groups between purine bases (the transglycosylation reaction) and are widely used for the synthesis of biologically important analogues of natural nucleosides, including a number of anticancer and antiviral drugs. Potent inhibitors of PNPs are used in chemotherapeutic applications. The detailed study of the binding of purine bases and their derivatives in the active site of PNPs is of particular interest in order to understand the mechanism of enzyme action and for the development of new enzyme inhibitors. Here, it is shown that 7-deazahypoxanthine (7DHX) is a noncompetitive inhibitor of the phosphorolysis of inosine by recombinant Escherichia coli PNP (EcPNP) with an inhibition constant K
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