Evidence map›Paper›PMID 38755143›Full record

ArticleNature communications2024

Structure, mechanism, and evolution of the last step in vitamin C biosynthesis.

Alessandro Boverio, Neelam Jamil, Barbara Mannucci, Maria Laura Mascotti, Marco W Fraaije, Andrea Mattevi

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Crystal structure of rice L-galactose dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. C11orf54 catalyzes L-xylulose formation in human metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Alessandro BoverioMolecular Enzymology group, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands.
Neelam JamilDepartment of Biology and Biotechnology, University of Pavia, via Ferrata 9, 27100, Pavia, Italy.ORCID http://orcid.org/0000-0001-8624-3326
Barbara MannucciCentro Grandi Strumenti, University of Pavia, Via Bassi 21, 27100, Pavia, Italy.ORCID http://orcid.org/0000-0002-7371-7243
Maria Laura MascottiMolecular Enzymology group, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands. mlmascotti@mendoza-conicet.gob.ar.ORCID http://orcid.org/0000-0002-5817-4631
Marco W FraaijeMolecular Enzymology group, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands. m.w.fraaije@rug.nl.ORCID http://orcid.org/0000-0001-6346-5014
Andrea MatteviDepartment of Biology and Biotechnology, University of Pavia, via Ferrata 9, 27100, Pavia, Italy. andrea.mattevi@unipv.it.ORCID http://orcid.org/0000-0002-9523-7128

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) MetaQ, No. 101094471EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) B-Ligzymes, GA 824017EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) COFUND project oLife No 847675
6 · The paper itself

Abstract

Photosynthetic organisms, fungi, and animals comprise distinct pathways for vitamin C biosynthesis. Besides this diversity, the final biosynthetic step consistently involves an oxidation reaction carried out by the aldonolactone oxidoreductases. Here, we study the origin and evolution of the diversified activities and substrate preferences featured by these flavoenzymes using molecular phylogeny, kinetics, mutagenesis, and crystallographic experiments. We find clear evidence that they share a common ancestor. A flavin-interacting amino acid modulates the reactivity with the electron acceptors, including oxygen, and determines whether an enzyme functions as an oxidase or a dehydrogenase. We show that a few side chains in the catalytic cavity impart the reaction stereoselectivity. Ancestral sequence reconstruction outlines how these critical positions were affixed to specific amino acids along the evolution of the major eukaryotic clades. During Eukarya evolution, the aldonolactone oxidoreductases adapted to the varying metabolic demands while retaining their overarching vitamin C-generating function.

Indexed as

Ascorbic AcidEvolution, MolecularPhylogenyAnimalsCatalytic DomainCrystallography, X-RayKineticsModels, MolecularOxidation-ReductionOxidoreductasesSubstrate SpecificityAscorbic AcidOxidoreductases

Identifiers

PMID38755143
PMCPMC11099136

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Registered trials

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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.