Evidence map›Paper›PMID 23826231›Full record

ArticlePloS one2013

Screening and Improving the Recombinant Nitrilases and Application in Biotransformation of Iminodiacetonitrile to Iminodiacetic Acid.

Zhi-Qiang Liu, Peter James Baker, Feng Cheng, Ya-Ping Xue, Yu-Guo Zheng, Yin-Chu Shen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

4 citing papers in PubMed, 30 citations in OpenAlex.

  1. Cyanide Biodegradation byMolecules (Basel, Switzerland) · 2022
    Article
  2. Potential of the Signal Peptide Derived from theApplied and environmental microbiology · 2022
    Article
  3. Review
  4. 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 1 institution in 1 country.

Zhi-Qiang LiuInstitute of Bioengineering, Zhejiang University of Technology, Hangzhou, People's Republic of China.
Peter James Baker
Feng Cheng
Ya-Ping Xue
Yu-Guo Zheng
Yin-Chu Shen
Zhejiang University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, several nitrilase genes from phylogenetically distinct organisms were expressed and purified in E. coli in order to study their ability to mediate the biotransformation of nitriles. We identified three nitrilases: Acidovorax facilis nitrilase (AcN); Alcaligenes fecalis nitrilase (AkN); and Rhodococcus rhodochrous nitrilase (RkN), which catalyzed iminodiacetonitrile (IDAN) to iminodiacetic acid (IDA). AcN demonstrated 8.8-fold higher activity for IDAN degradation as compared to AkN and RkN. Based on homology modeling and previously described 'hot spot' mutations, several AcN mutants were screened for improved activity. One mutant M3 (F168V/L201N/S192F) was identified, which demonstrates a 41% enhancement in the conversion as well as a 2.4-fold higher catalytic efficiency towards IDAN as compared to wild-type AcN.

Indexed as

AcetonitrilesAlcaligenes faecalisAminohydrolasesBacterial ProteinsBiotransformationChromatography, High Pressure LiquidCircular DichroismComamonadaceaeEscherichia coliHydrolysisImino AcidsKineticsMolecular Docking SimulationMutationProtein Structure, SecondaryRecombinant ProteinsAcetonitrilesAminohydrolasesBacterial ProteinsImino Acidsiminodiacetic acidnitrilaseRecombinant Proteins

Identifiers

PMID23826231
PMCPMC3695085
OpenAlexW1966687232

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.