Evidence map›Paper›PMID 23949008›Full record

ArticleMarine biotechnology (New York, N.Y.)2013

Characterisation of an L-haloacid dehalogenase from the marine psychrophile Psychromonas ingrahamii with potential industrial application.

Halina R Novak, Christopher Sayer, Jana Panning, Jennifer A Littlechild

Abstract read
PubMed Publisher
In one paragraph

Article in Marine biotechnology (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.8field-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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Temperature adaptation of DNA ligases from psychrophilic organisms.Extremophiles : life under extreme conditions · 2019
    Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Enzymes from Extreme Environments and Their Industrial Applications.Frontiers in bioengineering and biotechnology · 2015
    Review
  14. Review
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.

Halina R NovakThe Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK.
Christopher Sayer
Jana Panning
Jennifer A Littlechild
University of Exeter · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

The recombinant L-haloacid dehalogenase from the marine bacterium Psychromonas ingrahamii has been cloned and over-expressed in Escherichia coli. It shows activity towards monobromoacetic (100 %), monochloroacetic acid (62 %), S-chloropropionic acid (42 %), S-bromopropionic acid (31 %), dichloroacetic acid (28 %) and 2-chlorobutyric acid (10 %), respectively. The L-haloacid dehalogenase has highest activity towards substrates with shorter carbon chain lengths (≤ C3), without preference towards a chlorine or bromine at the α-carbon position. Despite being isolated from a psychrophilic bacterium, the enzyme has mesophilic properties with an optimal temperature for activity of 45 °C. It retains above 70 % of its activity after being incubated at 65 °C for 90 min before being assayed at 25 °C. The enzyme is relatively stable in organic solvents as demonstrated by activity and thermal shift analysis. The V max and K m were calculated to be 0.6 μM min(-1) mg(-1) and 1.36 mM with monobromoacetic acid, respectively. This solvent-resistant and stable L-haloacid dehalogenase from P. ingrahamii has potential to be used as a biocatalyst in industrial processes.

Indexed as

Models, MolecularProtein ConformationAcetatesAmino Acid SequenceBase SequenceBiocatalysisCloning, MolecularComputational BiologyDichloroacetic AcidDNA PrimersEscherichia coliGammaproteobacteriaHydrolasesIndustrial MicrobiologyMolecular Sequence DataPropionates2-haloacid dehalogenaseAcetatesbromoacetatechloroacetic acidDichloroacetic AcidDNA PrimersHydrolasesPropionatespropionic acid

Identifiers

PMID23949008
OpenAlexW1986460673

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.