Evidence map›Paper›PMID 28939805›Full record

ArticleScientific reports2017

Kynurenine aminotransferase activity of Aro8/Aro9 engage tryptophan degradation by producing kynurenic acid in Saccharomyces cerevisiae.

Kazuto Ohashi, Romanas Chaleckis, Masak Takaine, Craig E Wheelock, Satoshi Yoshida

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Compounds Derived from Tryptophan Metabolism inInternational journal of molecular sciences · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Honey's Yeast-New Source of Valuable Species for Industrial Applications.International journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Serum Metabolomics Analysis for Biomarkers ofFoods (Basel, Switzerland) · 2022
    Article
  12. The microbial production of kynurenic acid usingFrontiers in bioengineering and biotechnology · 2022
    Article
  13. Tryptophan Derivatives byInternational journal of molecular sciences · 2021
    Article
  14. NADFrontiers in molecular biosciences · 2021
    Review
  15. Review
  16. Article
  17. Article
  18. Proteomic Analysis ofMolecules (Basel, Switzerland) · 2020
    Article
  19. Cross-talk in NADCurrent genetics · 2019
    Review
  20. 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

5 authors at 1 institution in 2 countries.

Kazuto OhashiInstitute for Molecular and Cellular Regulation, Gunma University, Gunma, Japan. ohashi@gunma-u.ac.jp.
Romanas ChaleckisGunma University Initiative for Advanced Research (GIAR), Gunma University, Gunma, Japan.ORCID 0000-0001-8042-1005
Masak TakaineInstitute for Molecular and Cellular Regulation, Gunma University, Gunma, Japan.
Craig E WheelockGunma University Initiative for Advanced Research (GIAR), Gunma University, Gunma, Japan.
Satoshi YoshidaInstitute for Molecular and Cellular Regulation, Gunma University, Gunma, Japan.
Gunma University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kynurenic acid (KA) is a tryptophan (Trp) metabolite that is synthesised in a branch of kynurenine (KYN) pathway. KYN aminotransferase (KAT) catalyses deamination of KYN, yielding KA. Although KA synthesis is evolutionarily conserved from bacteria to humans, the cellular benefits of synthesising KA are unclear. In this study, we constructed a KAT-null yeast mutant defective in KA synthesis to clarify the cellular function of KA. Amino acid sequence analysis and LC/MS quantification of KA revealed that Aro8 and Aro9 are the major KATs. KA was significantly decreased in the aro8Δ aro9Δ double mutant. We found that aro8Δ aro9Δ cells did not exhibit obvious defects in growth or oxidative stress response when proper amounts of amino acids are supplied in the media. We further found that aro8Δ aro9Δ cells were sensitive to excess Trp. The Trp sensitivity was not rescued by addition of KA, suggesting that Trp sensitivity is not due to the loss of KA. In conclusion, we propose that KAT activity is required for detoxification of Trp by converting it to the less toxic KA.

Indexed as

Kynurenic AcidMutagenesisMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransaminasesTryptophanARO8 protein, S cerevisiaearomatic aminotransferase II, S cerevisiaeKynurenic AcidSaccharomyces cerevisiae ProteinsTransaminasesTryptophan

Identifiers

PMID28939805
PMCPMC5610271
OpenAlexW2756290026

What OpenQuestion holds

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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.