Evidence map›Paper›PMID 27189775›Full record

ArticleScientific reports2016

A novel pathway for fungal D-glucuronate catabolism contains an L-idonate forming 2-keto-L-gulonate reductase.

Joosu Kuivanen, Maura H Sugai-Guérios, Mikko Arvas, Peter Richard

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. The genome-scale sugar metabolic model fromCurrent research in microbial sciences · 2026
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  2. C11orf54 catalyzes L-xylulose formation in human metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  4. Unveiling new features of the human pathogenComputational and structural biotechnology journal · 2025
    Article
  5. Fermented foods and gastrointestinal health: underlying mechanisms.Nature reviews. Gastroenterology & hepatology · 2024
    Review
  6. Use of ambrAMB Express · 2022
    Article
  7. Article
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  9. Review
  10. Article
  11. Article
  12. Frontiers in cellular and infection microbiology · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. 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 at 2 institutions in 2 countries.

Joosu KuivanenVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044-VTT, Finland.
Maura H Sugai-GuériosDepartamento de Engenharia Química e Engenharia de Alimentos, Universidade Federal de Santa Catarina, Cx.P. 476 Centro Tecnológico, Florianópolis 88040-900, Santa Catarina, Brazil.
Mikko ArvasVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044-VTT, Finland.
Peter RichardVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044-VTT, Finland.
VTT Technical Research Centre of Finland · FIUniversidade Federal de Santa Catarina · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the catabolism of D-glucuronate, different pathways are used by different life forms. The pathways in bacteria and animals are established, however, a fungal pathway has not been described. In this communication, we describe an enzyme that is essential for D-glucuronate catabolism in the filamentous fungus Aspergillus niger. The enzyme has an NADH dependent 2-keto-L-gulonate reductase activity forming L-idonate. The deletion of the corresponding gene, the gluC, results in a phenotype of no growth on D-glucuronate. The open reading frame of the A. niger 2-keto-L-gulonate reductase was expressed as an active protein in the yeast Saccharomyces cerevisiae. A histidine tagged protein was purified and it was demonstrated that the enzyme converts 2-keto-L-gulonate to L-idonate and, in the reverse direction, L-idonate to 2-keto-L-gulonate using the NAD(H) as cofactors. Such an L-idonate forming 2-keto-L-gulonate dehydrogenase has not been described previously. In addition, the finding indicates that the catabolic D-glucuronate pathway in A. niger differs fundamentally from the other known D-glucuronate pathways.

Indexed as

Aspergillus nigerCarbohydrate DehydrogenasesFungal ProteinsGlucuronatesMetabolic Networks and PathwaysSaccharomyces cerevisiaeStereoisomerismSugar AcidsCarbohydrate DehydrogenasesFungal ProteinsGlucuronatesgulonic acididonic acidSugar Acids

Identifiers

PMID27189775
PMCPMC4870679
OpenAlexW2396986089

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.