Evidence map›Paper›PMID 24391356›Full record

ArticleBioinformation2013

insilico Characterization and Homology Modeling of Arabitol Dehydrogenase (ArDH) from Candida albican.

Muhammad Waseem Sarwar, Irum Baddisha Saleem, Asif Ali, Farhat Abbas

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Article in Bioinformation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 6 citations in OpenAlex.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Muhammad Waseem SarwarDepartment of Bioinformatics and Biotechnology, Government College University (GCU), Faisalabad, Pakistan.
Irum Baddisha SaleemDepartment of Bioinformatics and Biotechnology, Government College University (GCU), Faisalabad, Pakistan.
Asif AliDepartment of Bioinformatics and Biotechnology, Government College University (GCU), Faisalabad, Pakistan.
Farhat AbbasDepartment of Bioinformatics and Biotechnology, Government College University (GCU), Faisalabad, Pakistan.
Government College University, Faisalabad · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundArabitol dehydrogenase (ArDH) is involved in the production of different sugar alcohols like arabitol, sorbitol, mannitol, erythritol and xylitol by using five carbon sugars as substrate. Arabinose, d-ribose, d-ribulose, xylose and d-xylulose are known substrate of this enzyme. ArDH is mainly produced by osmophilic fungi for the conversion of ribulose to arabitol under stress conditions. Recently this enzyme has been used by various industries for the production of pharmaceutically important sugar alcohols form cheap source than glucose. But the information at structure level as well as its binding energy analysis with different substrates was missing.

resultsThe present study was focused on sequence analysis, insilico characterization and substrate binding analysis of ArDH from a fungus specie candida albican. Sequence analysis and physicochemical properties showed that this protein is highly stable, negatively charged and having more hydrophilic regions, these properties made this enzyme to bind with number of five carbon sugars as substrate. The predicted 3D model will helpful for further structure based studies. Docking analysis provided free energies of binding of each substrate from a best pose as arabinose -9.8224calK/mol, dribose -11.3701Kcal/mol, d-ribulose -8.9230Kcal/mol, xylose -9.7007Kcal/mol and d-xylulose 9.7802Kcal/mol.

conclusionOur study provided insight information of structure and interactions of ArDH with its substrate. These results obtained from this study clearly indicate that d-ribose is best substrate for ArDH for the production of sugar alcohols. This information will be helpful for better usage of this enzyme for hyper-production of sugar alcohols by different industries.

Indexed as

Arabitol dehydrogenaseCharaterizationHomology ModelinginsilicoMolecular Docking

Identifiers

PMID24391356
PMCPMC3867646
OpenAlexW2041262449

What OpenQuestion holds

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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.