Evidence map›Paper›PMID 27247428›Full record

ArticleBioscience reports2016

Molecular characterization of human ABHD2 as TAG lipase and ester hydrolase.

Naresh Kumar M, Thunuguntla V B S C, Veeramachaneni G K, Chandra Sekhar B, Swapna Guntupalli, Bondili J S

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Naresh Kumar MDepartment of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur District, Andhra Pradesh 522 502, India.
Thunuguntla V B S CDepartment of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur District, Andhra Pradesh 522 502, India.
Veeramachaneni G KDepartment of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur District, Andhra Pradesh 522 502, India.
Chandra Sekhar BDepartment of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur District, Andhra Pradesh 522 502, India.
Swapna GuntupalliDepartment of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur District, Andhra Pradesh 522 502, India.
Bondili J SDepartment of Biotechnology, K L University, Green fields, Vaddeswaram, Guntur District, Andhra Pradesh 522 502, India jksingh@kluniversity.in.
Koneru Lakshmaiah Education Foundation · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alterations in lipid metabolism have been progressively documented as a characteristic property of cancer cells. Though, human ABHD2 gene was found to be highly expressed in breast and lung cancers, its biochemical functionality is yet uncharacterized. In the present study we report, human ABHD2 as triacylglycerol (TAG) lipase along with ester hydrolysing capacity. Sequence analysis of ABHD2 revealed the presence of conserved motifs G(205)XS(207)XG(209) and H(120)XXXXD(125) Phylogenetic analysis showed homology to known lipases, Drosophila melanogaster CG3488. To evaluate the biochemical role, recombinant ABHD2 was expressed in Saccharomyces cerevisiae using pYES2/CT vector and His-tag purified protein showed TAG lipase activity. Ester hydrolase activity was confirmed with pNP acetate, butyrate and palmitate substrates respectively. Further, the ABHD2 homology model was built and the modelled protein was analysed based on the RMSD and root mean square fluctuation (RMSF) of the 100 ns simulation trajectory. Docking the acetate, butyrate and palmitate ligands with the model confirmed covalent binding of ligands with the Ser(207) of the GXSXG motif. The model was validated with a mutant ABHD2 developed with alanine in place of Ser(207) and the docking studies revealed loss of interaction between selected ligands and the mutant protein active site. Based on the above results, human ABHD2 was identified as a novel TAG lipase and ester hydrolase.

Indexed as

AnimalsDrosophila melanogasterEstersHumansHydrolasesHydrolysisLipaseLipid MetabolismPhylogenySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsABHD2 protein, humanEstersHydrolasesLipaseSaccharomyces cerevisiae Proteinsester hydrolaselipid metabolismtriacylglycerol (TAG) lipaseα β hydrolase domain

Identifiers

PMID27247428
PMCPMC4945992
OpenAlexW2410427823

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Registered trials

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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.