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Cloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus

Overview of attention for article published in 3 Biotech, August 2018
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Title
Cloning and characterization of trehalase: a conserved glycosidase from oriental midge, Chironomus ramosus
Published in
3 Biotech, August 2018
DOI 10.1007/s13205-018-1376-y
Pubmed ID
Authors

Ekta Shukla, Leena Thorat, Ameya D. Bendre, Santosh Jadhav, Jayanta K. Pal, Bimalendu B. Nath, Sushama M. Gaikwad

Abstract

Insect trehalase is a multiferous enzyme, crucial for normal physiological functions as well as under stress conditions. In this report, we present a fundamental study of the trehalase gene segment (1587 bp) from Chironomus ramosus (CrTre) encoding for 529 amino acids, using appropriate bioinformatics tools. C. ramosus, a tropical midge is an emerging animal model to investigate the consequences of environmental stresses. We observed that CrTre belongs to GH family 37 in the CAZy database and possess 57-92% identity to dipteran trehalases. In silico characterization provided information regarding the structural, functional and evolutionary aspects of midge trehalase. In the phylogenetic tree, CrTre clustered with the soluble dipteran trehalases. Moreover, domain functional characterization of the deduced protein sequence by InterProScan (IPR001661), ProSite (PS00927 and PS00928) and Pfam (PF01204) indicated presence of highly conserved signature motifs which are important for the identification of trehalase superfamily. Furthermore, the instability index of CrTre was predicted to be < 40 suggesting its in vivo stability while, the high aliphatic index indicated towards its thermal stability (index value 71-81). The modelled 3D tertiary structure of CrTre depicts a (α/α)6 barrel toroidal core. The catalytic domain of the enzyme comprised Glu424 and Asp226 as the putative active site residues. Interestingly, the conserved motifs were observed to be formed by the flexible loopy regions in the tertiary structure. This study revealed essential sequence features of the midge trehalase and offers better insights into the structural aspects of this enzyme which can be correlated with its function.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 9 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 9 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 3 33%
Student > Doctoral Student 3 33%
Professor 1 11%
Student > Master 1 11%
Unknown 1 11%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 44%
Agricultural and Biological Sciences 1 11%
Chemistry 1 11%
Unknown 3 33%
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 11 August 2018.
All research outputs
#20,529,980
of 23,099,576 outputs
Outputs from 3 Biotech
#821
of 1,252 outputs
Outputs of similar age
#288,930
of 331,040 outputs
Outputs of similar age from 3 Biotech
#30
of 50 outputs
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