Evidence map›Paper›PMID 16820480›Full record

ArticleApplied and environmental microbiology2006

Purification and characterization of two enantioselective alpha-ketoglutarate-dependent dioxygenases, RdpA and SdpA, from Sphingomonas herbicidovorans MH.

Tina A Müller, Thomas Fleischmann, Jan Roelof van der Meer, Hans-Peter E Kohler

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Isolation and 2,4-D-degrading characteristics of Cupriavidus campinensis BJ71.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2015
    Article
  8. Article
  9. Review
  10. Robust crop resistance to broadleaf and grass herbicides provided by aryloxyalkanoate dioxygenase transgenes.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. Article
  12. Article
  13. 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

4 authors at 1 institution in 1 country.

Tina A MüllerSwiss Federal Institute of Aquatic Science and Technology (Eawag), Uberlandstrasse 133, CH-8600 Dübendorf, Switzerland.
Thomas Fleischmann
Jan Roelof van der Meer
Hans-Peter E Kohler
Swiss Federal Institute of Aquatic Science and Technology · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase (RdpA) and alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase (SdpA), which are involved in the degradation of phenoxyalkanoic acid herbicides in Sphingomonas herbicidovorans MH, were expressed and purified as His6-tagged fusion proteins from Escherichia coli BL21(DE3)(pLysS). RdpA and SdpA belong to subgroup II of the alpha-ketoglutarate-dependent dioxygenases and share the specific motif HXDX(24)TX(131)HX(10)R. Amino acids His-111, Asp-113, and His-270 and amino acids His-102, Asp-104, and His 257 comprise the 2-His-1-carboxylate facial triads and were predicted to be involved in iron binding in RdpA and SdpA, respectively. RdpA exclusively transformed the (R) enantiomers of mecoprop [2-(4-chloro-2-methylphenoxy)propanoic acid] and dichlorprop [2-(2,4-dichlorophenoxy)propanoic acid], whereas SdpA was specific for the (S) enantiomers. The apparent Km values were 99 microM for (R)-mecoprop, 164 microM for (R)-dichlorprop, and 3 microM for alpha-ketoglutarate for RdpA and 132 microM for (S)-mecoprop, 495 microM for (S)-dichlorprop, and 20 microM for alpha-ketoglutarate for SdpA. Both enzymes had high apparent Km values for oxygen; these values were 159 microM for SdpA and >230 microM for RdpA, whose activity was linearly dependent on oxygen at the concentration range measured. Both enzymes had narrow cosubstrate specificity; only 2-oxoadipate was able to replace alpha-ketoglutarate, and the rates were substantially diminished. Ferrous iron was necessary for activity of the enzymes, and other divalent cations could not replace it. Although the results of growth experiments suggest that strain MH harbors a specific 2,4-dichlorophenoxyacetic acid-converting enzyme, tfdA-, tfdAalpha-, or cadAB-like genes were not discovered in a screening analysis in which heterologous hybridization and PCR were used.

Indexed as

2,4-Dichlorophenoxyacetic Acid2-Methyl-4-chlorophenoxyacetic AcidAmino Acid SequenceDioxygenasesEscherichia coliHerbicidesKetoglutaric AcidsMixed Function OxygenasesMolecular Sequence DataRecombinant Fusion ProteinsSphingomonasStereoisomerismSubstrate Specificity2,4-Dichlorophenoxyacetic Acid2-Methyl-4-chlorophenoxyacetic Acidalpha-ketoglutarate 2-(2,4-dichlorophenoxy)propionate dioxygenasedichlorpropDioxygenasesHerbicidesKetoglutaric AcidsmecopropMixed Function OxygenasesRecombinant Fusion Proteins

Identifiers

PMID16820480
PMCPMC1489315
OpenAlexW2059379861

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.