Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.

Denis Smyshliaev, Martin Pfeiffer, Udo Oppermann, Bernd Nidetzky

Abstract read

In one paragraph

Article in ACS catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Probing the Human 4-Oxo-l-proline Reductase-Catalyzed Reaction by Deuterium Kinetic and Equilibrium Isotope Effects.Biochemistry · 2026
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

4 authors.

Denis SmyshliaevInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, A-8010 Graz, Austria.

Martin PfeifferInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, A-8010 Graz, Austria.

Udo OppermannBotnar Research Centre, Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, National Institute of Health Research Oxford Biomedical Research Unit (BRU), University of Oxford, OX3 7LD Oxford, U.K.

Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Petersgasse 12, A-8010 Graz, Austria.ORCID https://orcid.org/0000-0002-5030-2643

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GDP-l-fucose is a universal sugar donor for the cellular biosynthesis of l-fucose-containing glycans. Its supply comes primarily from the reaction of GDP-l-fucose synthase (GFS), also known as GDP-4″-keto-6″-deoxy-d-mannose epimerase/reductase. GFS converts GDP-4″-keto-6″-deoxy-d-mannose by epimerization at both C-3″ and C-5″ followed by NADPH-dependent reduction of the carbonyl at C-4″. Here, we report kinetic and structural characterization of human GFS with the aim of dissecting the multistep pathway of the enzymatic reaction. Kinetic isotope effects due to [3″-

Indexed as

enzyme mechanismfucosylationGDP-4″-keto-6″-deoxy-d-mannose epimerase/reductaseGDP-l-fucoseGDP-l-fucose synthase (GFS)kinetic isotope effectsmultistep kinetic pathway

Identifiers

PMID40837376

DOI10.1021/acscatal.5c02722

PMCPMC12362431

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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.