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RETRACTED ARTICLE: Substrates specificity of tannase from Streptomyces sviceus and Lactobacillus plantarum

Overview of attention for article published in AMB Express, September 2018
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  • Good Attention Score compared to outputs of the same age and source (70th percentile)

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Title
RETRACTED ARTICLE: Substrates specificity of tannase from Streptomyces sviceus and Lactobacillus plantarum
Published in
AMB Express, September 2018
DOI 10.1186/s13568-018-0677-1
Pubmed ID
Authors

Dan Wang, Yao Liu, Die Lv, Xueli Hu, Qiumei Zhong, Ye Zhao, Mingbo Wu

Abstract

Tannases can catalyze the hydrolysis of galloyl ester and depside bonds of hydrolysable tannins to release gallic acid and glucose, but tannases from different species have different substrate specificities. Our prior studies found that tannase from Lactobacillus plantarum (LP-tan) performed a higher esterase activity, while the tannase from Streptomyces sviceus (SS-tan) performed a higher depsidase activity; but the molecular mechanism is not elucidated. Based on the crystal structure of LP-tan and the amino acid sequences alignment between LP-tan and SS-tan, we found that the sandwich structure formed by Ile206-substrate-Pro356 in LP-tan was replaced with Ile253-substrate-Gly384 in SS-tan, and the flap domain (amino acids: 225-247) formed in LP-tan was missed in SS-tan, while a flap-like domain (amino acids: 93-143) was found in SS-tan. In this study, we investigated the functional role of sandwich structure and the flap (flap-like) domain in the substrate specificity of tannase. Site-directed mutagenesis was used to disrupt the sandwich structure in LP-tan (P356G) and rebuilt it in SS-tan (G384P). The flap in LP-tan and the flap-like domain in SS-tan were deleted to construct the new variants. The activity assay results showed that the sandwich and the flap domain can help to catalytic the ester bonds, while the flap-like domain in SS-tan mainly worked on the depside bonds. Enzymatic characterization and kinetics data showed that the sandwich and the flap domain can help to catalytic the ester bonds, while the flap-like domain in SS-tan may worked on the depside bonds.

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Mendeley readers

Mendeley readers

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Geographical breakdown

Country Count As %
Unknown 12 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 3 25%
Professor 1 8%
Other 1 8%
Unknown 7 58%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 17%
Immunology and Microbiology 1 8%
Unknown 9 75%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. 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 22 April 2019.
All research outputs
#17,990,409
of 23,103,903 outputs
Outputs from AMB Express
#740
of 1,245 outputs
Outputs of similar age
#245,150
of 342,003 outputs
Outputs of similar age from AMB Express
#15
of 57 outputs
Altmetric has tracked 23,103,903 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 1,245 research outputs from this source. They receive a mean Attention Score of 2.8. This one is in the 35th percentile – i.e., 35% 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 342,003 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 23rd percentile – i.e., 23% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 57 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 70% of its contemporaries.