Evidence map›Paper›PMID 26729714›Full record

ArticleApplied and environmental microbiology2016

Nicotine Dehydrogenase Complexed with 6-Hydroxypseudooxynicotine Oxidase Involved in the Hybrid Nicotine-Degrading Pathway in Agrobacterium tumefaciens S33.

Huili Li, Kebo Xie, Wenjun Yu, Liejie Hu, Haiyan Huang, Huijun Xie, Shuning Wang

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Rational Design of a Flavoenzyme for Aerobic Nicotine Catabolism.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The Antioxidant Properties of Alfalfa (Oxidative medicine and cellular longevity · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. The enzymes of microbial nicotine metabolism.Beilstein journal of organic chemistry · 2018
    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

7 authors at 3 institutions in 1 country.

Huili LiState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Kebo XieState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Wenjun YuState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Liejie HuState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Haiyan HuangInstitute of Basic Medicine, Shandong Academy of Medical Science, Jinan, People's Republic of China.
Huijun XieEnvironment Research Institute, Shandong University, Jinan, People's Republic of China.
Shuning WangState Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China shuningwang@sdu.edu.cn.
Shandong University · CNState Key Laboratory of Microbial TechnologyShandong First Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nicotine, a major toxic alkaloid in tobacco wastes, is degraded by bacteria, mainly via pyridine and pyrrolidine pathways. Previously, we discovered a new hybrid of the pyridine and pyrrolidine pathways in Agrobacterium tumefaciens S33 and characterized its key enzyme 6-hydroxy-3-succinoylpyridine (HSP) hydroxylase. Here, we purified the nicotine dehydrogenase initializing the nicotine degradation from the strain and found that it forms a complex with a novel 6-hydroxypseudooxynicotine oxidase. The purified complex is composed of three different subunits encoded by ndhAB and pno, where ndhA and ndhB overlap by 4 bp and are ∼26 kb away from pno. As predicted from the gene sequences and from chemical analyses, NdhA (82.4 kDa) and NdhB (17.1 kDa) harbor a molybdopterin cofactor and two [2Fe-2S] clusters, respectively, whereas Pno (73.3 kDa) harbors an flavin mononucleotide and a [4Fe-4S] cluster. Mutants with disrupted ndhA or ndhB genes did not grow on nicotine but grew well on 6-hydroxynicotine and HSP, whereas the pno mutant did not grow on nicotine or 6-hydroxynicotine but grew well on HSP, indicating that NdhA and NdhB are responsible for initialization of nicotine oxidation. We successfully expressed pno in Escherichia coli and found that the recombinant Pno presented 2,6-dichlorophenolindophenol reduction activity when it was coupled with 6-hydroxynicotine oxidation. The determination of reaction products catalyzed by the purified enzymes or mutants indicated that NdhAB catalyzed nicotine oxidation to 6-hydroxynicotine, whereas Pno oxidized 6-hydroxypseudooxynicotine to 6-hydroxy-3-succinoylsemialdehyde pyridine. These results provide new insights into this novel hybrid pathway of nicotine degradation in A. tumefaciens S33.

Indexed as

Metabolic Networks and PathwaysAgrobacterium tumefaciensAmino Acid MotifsBiotransformationEscherichia coliGene ExpressionGene Knockout TechniquesMolecular WeightMultienzyme ComplexesNicotineOxidoreductasesOxidoreductases Acting on CH-NH Group DonorsMultienzyme ComplexesNicotinenicotine dehydrogenaseOxidoreductasesOxidoreductases Acting on CH-NH Group Donors

Identifiers

PMID26729714
PMCPMC4784044
OpenAlexW2229595559

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.