Evidence map›Paper›PMID 28294121›Full record

ArticleScientific reports2017

A bacterial aromatic aldehyde dehydrogenase critical for the efficient catabolism of syringaldehyde.

Naofumi Kamimura, Takayuki Goto, Kenji Takahashi, Daisuke Kasai, Yuichiro Otsuka, Masaya Nakamura, Yoshihiro Katayama, Masao Fukuda, Eiji Masai

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Platform Potential ofJournal of agricultural and food chemistry · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. The catabolism of lignin-derivedApplied and environmental microbiology · 2024
    Article
  7. Article
  8. [ALDH3B1 expression is correlated with histopathology and long-term prognosis of gastric cancer].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Lignin valorization meets synthetic biology.Engineering in life sciences · 2019
    Review
  17. Article
  18. Article
  19. Article
  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

9 authors at 3 institutions in 1 country.

Naofumi KamimuraDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Takayuki GotoDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Kenji TakahashiDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Daisuke KasaiDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Yuichiro OtsukaForestry and Forest Products Research Institute, Tsukuba, Ibaraki 305-8687, Japan.
Masaya NakamuraForestry and Forest Products Research Institute, Tsukuba, Ibaraki 305-8687, Japan.
Yoshihiro KatayamaCollege of Bioresource Sciences, Nihon University, Fujisawa, Kanagawa 252-0880, Japan.
Masao FukudaDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Eiji MasaiDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Nagaoka University of Technology · JPForestry and Forest Products Research Institute · JPNihon University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vanillin and syringaldehyde obtained from lignin are essential intermediates for the production of basic chemicals using microbial cell factories. However, in contrast to vanillin, the microbial conversion of syringaldehyde is poorly understood. Here, we identified an aromatic aldehyde dehydrogenase (ALDH) gene responsible for syringaldehyde catabolism from 20 putative ALDH genes of Sphingobium sp. strain SYK-6. All these genes were expressed in Escherichia coli, and nine gene products, including previously characterized BzaA, BzaB, and vanillin dehydrogenase (LigV), exhibited oxidation activities for syringaldehyde to produce syringate. Among these genes, SLG_28320 (desV) and ligV were most highly and constitutively transcribed in the SYK-6 cells. Disruption of desV in SYK-6 resulted in a significant reduction in growth on syringaldehyde and in syringaldehyde oxidation activity. Furthermore, a desV ligV double mutant almost completely lost its ability to grow on syringaldehyde. Purified DesV showed similar k

Indexed as

PhylogenyAldehyde DehydrogenaseAldehyde OxidoreductasesBenzaldehydesEscherichia coliMetabolismMultigene FamilySphingomonadaceaeAldehyde DehydrogenaseAldehyde OxidoreductasesBenzaldehydessyringaldehydevanillinvanillin dehydrogenase

Identifiers

PMID28294121
PMCPMC5353671
OpenAlexW2653547707

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.