Evidence map›Paper›PMID 24123738›Full record

ArticleApplied and environmental microbiology2013

The novel bacterial N-demethylase PdmAB is responsible for the initial step of N,N-dimethyl-substituted phenylurea herbicide degradation.

Tao Gu, Chaoyang Zhou, Sebastian R Sørensen, Ji Zhang, Jian He, Peiwen Yu, Xin Yan, Shunpeng Li

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2013. 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
1.8field-weighted citation impact, top 16% 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, 51 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Carbamate C-N Hydrolase GeneApplied and environmental microbiology · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. An Amidase Gene,Applied and environmental microbiology · 2018
    Article
  15. Article
  16. Article
  17. Isolation and characterization of Bradyrhizobium sp. SR1 degrading two β-triketone herbicides.Environmental science and pollution research international · 2016
    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

8 authors at 2 institutions in 2 countries.

Tao GuDepartment of Microbiology, College of Life Sciences, Key Laboratory for Microbiological Engineering of Agricultural Environment of Ministry of Agriculture, Nanjing Agricultural University, Nanjing, Jiangsu, People's Republic of China.
Chaoyang Zhou
Sebastian R Sørensen
Ji Zhang
Jian He
Peiwen Yu
Xin Yan
Shunpeng Li
Nanjing Agricultural University · CNGeological Survey of Denmark and Greenland · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The environmental fate of phenylurea herbicides has received considerable attention in recent decades. The microbial metabolism of N,N-dimethyl-substituted phenylurea herbicides can generally be initiated by mono-N-demethylation. In this study, the molecular basis for this process was revealed. The pdmAB genes in Sphingobium sp. strain YBL2 were shown to be responsible for the initial mono-N-demethylation of commonly used N,N-dimethyl-substituted phenylurea herbicides. PdmAB is the oxygenase component of a bacterial Rieske non-heme iron oxygenase (RO) system. The genes pdmAB, encoding the α subunit PdmA and the β subunit PdmB, are organized in a transposable element flanked by two direct repeats of an insertion element resembling ISRh1. Furthermore, this transposable element is highly conserved among phenylurea herbicide-degrading sphingomonads originating from different areas of the world. However, there was no evidence of a gene for an electron carrier (a ferredoxin or a reductase) located in the immediate vicinity of pdmAB. Without its cognate electron transport components, expression of PdmAB in Escherichia coli, Pseudomonas putida, and other sphingomonads resulted in a functional enzyme. Moreover, coexpression of a putative [3Fe-4S]-type ferredoxin from Sphingomonas sp. strain RW1 greatly enhanced the catalytic activity of PdmAB in E. coli. These data suggested that PdmAB has a low specificity for electron transport components and that its optimal ferredoxin may be the [3Fe-4S] type. PdmA exhibited low homology to the α subunits of previously characterized ROs (less than 37% identity) and did not cluster with the RO group involved in O- or N-demethylation reactions, indicating that PdmAB is a distinct bacterial RO N-demethylase.

Indexed as

BiotransformationCluster AnalysisDNA, BacterialElectron TransportEscherichia coliGene ExpressionHerbicidesMolecular Sequence DataOxidoreductases, N-DemethylatingPhenylurea CompoundsPhylogenyPseudomonas putidaSequence Analysis, DNASequence Homology, Amino AcidSphingomonadaceaeDNA, BacterialHerbicidesOxidoreductases, N-DemethylatingPhenylurea Compounds

Identifiers

PMID24123738
PMCPMC3837831
OpenAlexW2144901761

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.