Evidence map›Paper›PMID 25002425›Full record

ArticleApplied and environmental microbiology2014

A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7.

Jiguo Qiu, Yin Wei, Yun Ma, Rongti Wen, Yuezhong Wen, Weiping Liu

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 10% 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, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. The enzymes of microbial nicotine metabolism.Beilstein journal of organic chemistry · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

6 authors at 2 institutions in 1 country.

Jiguo QiuKey Laboratory of Environmental Remediation and Ecosystem Health, Ministry of Education, College of Environmental and Resource Sciences, Zhejiang University, Hangzhou, China.
Yin WeiResearch Center of Environmental Science, College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, China.
Yun MaResearch Center of Environmental Science, College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, China.
Rongti WenResearch Center of Environmental Science, College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou, China.
Yuezhong WenKey Laboratory of Environmental Remediation and Ecosystem Health, Ministry of Education, College of Environmental and Resource Sciences, Zhejiang University, Hangzhou, China.
Weiping LiuKey Laboratory of Environmental Remediation and Ecosystem Health, Ministry of Education, College of Environmental and Resource Sciences, Zhejiang University, Hangzhou, China wliu@zju.edu.cn.
Zhejiang University · CNZhejiang University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nicotine is an important environmental toxicant in tobacco waste. Shinella sp. strain HZN7 can metabolize nicotine into nontoxic compounds via variations of the pyridine and pyrrolidine pathways. However, the catabolic mechanism of this variant pathway at the gene or enzyme level is still unknown. In this study, two 6-hydroxynicotine degradation-deficient mutants, N7-M9 and N7-W3, were generated by transposon mutagenesis. The corresponding mutant genes, designated nctB and tnp2, were cloned and analyzed. The nctB gene encodes a novel flavin adenine dinucleotide-containing (S)-6-hydroxynicotine oxidase that converts (S)-6-hydroxynicotine into 6-hydroxy-N-methylmyosmine and then spontaneously hydrolyzes into 6-hydroxypseudooxynicotine. The deletion and complementation of the nctB gene showed that this enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation. Purified NctB could also convert (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzed into pseudooxynicotine. The kinetic constants of NctB toward (S)-6-hydroxynicotine (Km = 0.019 mM, kcat = 7.3 s(-1)) and nicotine (Km = 2.03 mM, kcat = 0.396 s(-1)) indicated that (S)-6-hydroxynicotine is the preferred substrate in vivo. NctB showed no activities toward the R enantiomer of nicotine or 6-hydroxynicotine. Strain HZN7 could degrade (R)-nicotine into (R)-6-hydroxynicotine without any further degradation. The tnp2 gene from mutant N7-W3 encodes a putative transposase, and its deletion did not abolish the nicotine degradation activity. This study advances the understanding of the microbial diversity of nicotine biodegradation.

Indexed as

DNA Transposable ElementsGene Knockout TechniquesGenetic Complementation TestKineticsMembrane GlycoproteinsMutagenesis, InsertionalNicotineOxidoreductasesRhizobiaceaeSubstrate Specificity6-hydroxynicotineDNA Transposable ElementsMembrane GlycoproteinsNicotineOxidoreductasesS-layer proteins

Identifiers

PMID25002425
PMCPMC4178596
OpenAlexW2000635250

What OpenQuestion holds

Textmetadata
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.