Crystal structure of L-2-keto-3-deoxyfuconate 4-dehydrogenase reveals a unique binding mode as a α-furanosyl hemiketal of substrates.

Miyu Akagashi, Seiya Watanabe, Sebastian Kwiatkowski, Jakub Drozak, Shin-Ichi Terawaki, Yasunori Watanabe

Abstract read

In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it

0cells of the map it votes in

3citing 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

3 citing papers in PubMed.

Orphan Enzymes in the Mammalian L-Fucose Degradation Pathway.Biomolecules · 2026
Review
Identification, functional characterization, and structural analysis of an atypical l-threonate 3-dehydrogenase.The Journal of biological chemistry · 2026
Article
Kinetic and Thermodynamic Characterization of Human 4-Oxo-l-proline Reductase Catalysis.Biochemistry · 2025
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.

Miyu Akagashi *Department of Bioscience, Graduate School of Agriculture, Ehime University, Matsuyama, Ehime, Japan.

Seiya Watanabe *Department of Bioscience, Graduate School of Agriculture, Ehime University, Matsuyama, Ehime, Japan. irab@agr.ehime-u.ac.jp.

Sebastian KwiatkowskiDepartment of Metabolic Regulation, Institute of Biochemistry, Faculty of Biology, University of Warsaw, Warsaw, Poland.

Jakub DrozakDepartment of Metabolic Regulation, Institute of Biochemistry, Faculty of Biology, University of Warsaw, Warsaw, Poland.

Shin-Ichi TerawakiDivision of Structure Analysis of Protein Complex, Proteo-Science Center (PROS), Ehime University, Matsuyama, Ehime, Japan.

Yasunori WatanabeFaculty of Science, Yamagata University, 1-4-12 Kojirakawa-machi, Yamagata, Yamagata, 990-8560, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-2-Keto-3-deoxyfuconate 4-dehydrogenase (L-KDFDH) catalyzes the NAD

Indexed as

Models, MolecularBacterial ProteinsBinding SitesCrystallography, X-RayProtein BindingSubstrate SpecificityBacterial Proteins2-keto-3-deoxysugar acidDehydrogenaseFuranosyl hemiketalMolecular evolutionShort-chain dehydrogenase/reductaseSubstrate specificity

Identifiers

PMID38918500

DOI10.1038/s41598-024-65627-8

PMCPMC11199699

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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.