ArticleChemical communications (Cambridge, England)2019
PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis.
Article in Chemical communications (Cambridge, England), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Antibiotic Mechanisms and Resistance: Molecular Insights and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2026Review
- Pyrazofurin Biosynthesis Involves Nonenzymatic Ring Contraction of a Pyridazine Intermediate Triggered by a Rieske Enzyme-Catalyzed Oxygenation.Journal of the American Chemical Society · 2025Article
- Advancing Covalent Ligand and Drug Discovery beyond Cysteine.Chemical reviews · 2025Review
- Revision of the Formycin A and Pyrazofurin Biosynthetic Pathways Reveals Specificity for d-Glutamic Acid and a CrypticJournal of the American Chemical Society · 2025Article
- Biosynthesis of C-nucleoside antibiotics in actinobacteria: recent advances and future developments.Microbial cell factories · 2022Review
- Substrate Reduction Therapy for Krabbe Disease: Exploring the Repurposing of the Antibiotic D-Cycloserine.Frontiers in pediatrics · 2021Article
- Uncovering the chemistry of C-C bond formation in C-nucleoside biosynthesis: crystal structure of a C-glycoside synthase/PRPP complex.Chemical communications (Cambridge, England) · 2020Article
- Whole-Genome Sequence ofMicrobiology resource announcements · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 6 institutions in 3 countries.
Funding
Abstract
ForI is a PLP-dependent enzyme from the biosynthetic pathway of the C-nucleoside antibiotic formycin. Cycloserine is thought to inhibit PLP-dependent enzymes by irreversibly forming a PMP-isoxazole. We now report that ForI forms novel PMP-diketopiperazine derivatives following incubation with both d and l cycloserine. This unexpected result suggests chemical diversity in the chemistry of cycloserine inhibition.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.