ArticleJournal of the American Chemical Society2026
Discovery of a Structurally Distinct Acetylenase in the Biosynthesis of Mangotoxin.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Beneath the Bark: Molecular Determinants of Adaptation and Infection in Bacterial Pathogens of Woody Hosts.Molecular plant pathology · 2026Review
- Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Amino acids, peptides, and proteins play pivotal roles in medicine, materials, and catalysis, with their functions largely dictated by their side-chain functionality. Recent studies have shown that heme oxygenase-like domain-containing oxidases (HDOs) catalyze a broad range of interesting chemical reactions on amino acids and their derivatives to produce structurally diverse target structures. Using a bioinformatics approach, the mangotoxin biosynthetic operon was found to house an unannotated HDO, MboA, along with a dedicated redox partner, MboB. We show that MboA catalyzes alkyne formation by iterative desaturations on the side-chain of a peptide substrate, where the transformation between alkene and alkyne is gated by MboB. The crystal structure of Fe(II)
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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.