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A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments

Overview of attention for article published in BMC Biotechnology, January 2015
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (86th percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

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1 news outlet
twitter
3 tweeters

Citations

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48 Dimensions

Readers on

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67 Mendeley
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Title
A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments
Published in
BMC Biotechnology, January 2015
DOI 10.1186/s12896-015-0115-2
Pubmed ID
Authors

Dae-Hee Lee, Su-Lim Choi, Eugene Rha, Soo Jin Kim, Soo-Jin Yeom, Jae-Hee Moon, Seung-Goo Lee

Abstract

BackgroundAlkaline phosphatase (AP) catalyzes the hydrolytic cleavage of phosphate monoesters under alkaline conditions and plays important roles in microbial ecology and molecular biology applications. Here, we report on the first isolation and biochemical characterization of a thermolabile AP from a metagenome.ResultsThe gene encoding a novel AP was isolated from a metagenomic library constructed with ocean-tidal flat sediments from the west coast of Korea. The metagenome-derived AP (mAP) gene composed of 1,824 nucleotides encodes a polypeptide with a calculated molecular mass of 64 kDa. The deduced amino acid sequence of mAP showed a high degree of similarity to other members of the AP family. Phylogenetic analysis revealed that the mAP is shown to be a member of a recently identified family of PhoX that is distinct from the well-studied classical PhoA family. When the open reading frame encoding mAP was cloned and expressed in recombinant Escherichia coli, the mature mAP was secreted to the periplasm and lacks an 81-amino-acid N-terminal Tat signal peptide. Mature mAP was purified to homogeneity as a monomeric enzyme with a molecular mass of 56 kDa. The purified mAP displayed typical features of a psychrophilic enzyme: high catalytic activity at low temperature and a remarkable thermal instability. The optimal temperature for the enzymatic activity of mAP was 37°C and complete thermal inactivation of the enzyme was observed at 65°C within 15 min. mAP was activated by Ca2+ and exhibited maximal activity at pH 9.0. Except for phytic acid and glucose 1-phosphate, mAP showed phosphatase activity against various phosphorylated substrates indicating that it had low substrate specificity. In addition, the mAP was able to remove terminal phosphates from cohesive and blunt ends of linearized plasmid DNA, exhibiting comparable efficiency to commercially available APs that have been used in molecular biology.ConclusionsThe presented mAP enzyme is the first thermolabile AP found in cold-adapted marine metagenomes and may be useful for efficient dephosphorylation of linearized DNA.

Twitter Demographics

The data shown below were collected from the profiles of 3 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 67 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
China 1 1%
Canada 1 1%
Unknown 65 97%

Demographic breakdown

Readers by professional status Count As %
Student > Master 16 24%
Student > Ph. D. Student 13 19%
Researcher 12 18%
Student > Bachelor 9 13%
Student > Doctoral Student 3 4%
Other 7 10%
Unknown 7 10%
Readers by discipline Count As %
Agricultural and Biological Sciences 30 45%
Biochemistry, Genetics and Molecular Biology 17 25%
Environmental Science 4 6%
Chemical Engineering 2 3%
Pharmacology, Toxicology and Pharmaceutical Science 2 3%
Other 6 9%
Unknown 6 9%

Attention Score in Context

This research output has an Altmetric Attention Score of 10. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 06 February 2015.
All research outputs
#468,389
of 4,781,719 outputs
Outputs from BMC Biotechnology
#64
of 403 outputs
Outputs of similar age
#23,248
of 169,753 outputs
Outputs of similar age from BMC Biotechnology
#13
of 24 outputs
Altmetric has tracked 4,781,719 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 90th percentile: it's in the top 10% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 403 research outputs from this source. They receive a mean Attention Score of 4.1. This one has done well, scoring higher than 79% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 169,753 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 86% of its contemporaries.
We're also able to compare this research output to 24 others from the same source and published within six weeks on either side of this one. This one is in the 41st percentile – i.e., 41% of its contemporaries scored the same or lower than it.