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Linalool isomerase, a membrane-anchored enzyme in the anaerobic monoterpene degradation in Thauera linaloolentis 47Lol

Overview of attention for article published in BMC Molecular and Cell Biology, March 2016
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About this Attention Score

  • Above-average Attention Score compared to outputs of the same age (54th percentile)
  • Good Attention Score compared to outputs of the same age and source (76th percentile)

Mentioned by

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1 Wikipedia page

Citations

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15 Dimensions

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33 Mendeley
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Title
Linalool isomerase, a membrane-anchored enzyme in the anaerobic monoterpene degradation in Thauera linaloolentis 47Lol
Published in
BMC Molecular and Cell Biology, March 2016
DOI 10.1186/s12858-016-0062-0
Pubmed ID
Authors

Robert Marmulla, Barbara Šafarić, Stephanie Markert, Thomas Schweder, Jens Harder

Abstract

Thauera linaloolentis 47Lol uses the tertiary monoterpene alcohol (R,S)-linalool as sole carbon and energy source under denitrifying conditions. The conversion of linalool to geraniol had been observed in carbon-excess cultures, suggesting the presence of a 3,1-hydroxyl-Δ(1)-Δ(2)-mutase (linalool isomerase) as responsible enzyme. To date, only a single enzyme catalyzing such a reaction is described: the linalool dehydratase/isomerase (Ldi) from Castellaniella defragrans 65Phen acting only on (S)-linalool. The linalool isomerase activity was located in the inner membrane. It was enriched by subcellular fractionation and sucrose gradient centrifugation. MALDI-ToF MS analysis of the enriched protein identified the corresponding gene named lis that codes for the protein in the strain with the highest similarity to the Ldi. Linalool isomerase is predicted to have four transmembrane helices at the N-terminal domain and a cytosolic domain. Enzyme activity required a reductant for activation. A specific activity of 3.42 ± 0.28 nkat mg * protein(-1) and a kM value of 455 ± 124 μM were determined for the thermodynamically favored isomerization of geraniol to both linalool isomers at optimal conditions of pH 8 and 35 °C. The linalool isomerase from T. linaloolentis 47Lol represents a second member of the enzyme class 5.4.4.4, next to the linalool dehydratase/isomerase from C. defragrans 65Phen. Besides considerable amino acid sequence similarity both enzymes share common characteristics with respect to substrate affinity, pH and temperature optima, but differ in the dehydratase activity and the turnover of linalool isomers.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 33 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 33 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 5 15%
Researcher 5 15%
Student > Ph. D. Student 4 12%
Student > Postgraduate 4 12%
Student > Bachelor 2 6%
Other 2 6%
Unknown 11 33%
Readers by discipline Count As %
Agricultural and Biological Sciences 7 21%
Biochemistry, Genetics and Molecular Biology 6 18%
Chemistry 3 9%
Immunology and Microbiology 2 6%
Medicine and Dentistry 2 6%
Other 3 9%
Unknown 10 30%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. 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 17 March 2016.
All research outputs
#8,534,528
of 25,373,627 outputs
Outputs from BMC Molecular and Cell Biology
#334
of 1,233 outputs
Outputs of similar age
#114,197
of 314,269 outputs
Outputs of similar age from BMC Molecular and Cell Biology
#4
of 17 outputs
Altmetric has tracked 25,373,627 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,233 research outputs from this source. They receive a mean Attention Score of 4.0. This one is in the 48th percentile – i.e., 48% of its peers scored the same or lower than it.
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 314,269 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 54% of its contemporaries.
We're also able to compare this research output to 17 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 76% of its contemporaries.