Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases
Halophiles are extremophilic microorganisms that grow optimally at high salt concentrations by producing a myriad of equally halotolerant enzymes. Structural haloadaptation of these enzymes adept to thriving under high-salt environments, though are not fully understood. Herein, the study attempts an...
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my.utm.923772021-09-28T07:43:46Z http://eprints.utm.my/id/eprint/92377/ Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases Edbeib, Mohamed Faraj Aksoy, Hasan Murat Kaya, Yilmaz Abdul Wahab, Roswanira Huyop, Fahrul QD Chemistry Halophiles are extremophilic microorganisms that grow optimally at high salt concentrations by producing a myriad of equally halotolerant enzymes. Structural haloadaptation of these enzymes adept to thriving under high-salt environments, though are not fully understood. Herein, the study attempts an in silico investigation to identify and comprehend the evolutionary structural adaptation of a halotolerant dehalogenase, DehHX (GenBank accession number: KR297065) of the halotolerant Pseudomonas halophila, over its non-halotolerant counterpart, DehMX1 (GenBank accession number KY129692) produced by Pseudomonas aeruginosa. GC content of the halotolerant DehHX DNA sequence was distinctively higher (58.9%) than the non-halotolerant dehalogenases (55% average GC). Its acidic residues, Asp and Glu were 8.27% and 12.06%, respectively, compared to an average 5.5% Asp and 7% Glu, in the latter; but lower contents of basic and hydrophobic residues in the DehHX. The secondary structure of DehHX interestingly revealed a lower incidence of α-helix forming regions (29%) and a higher percentage of coils (57%), compared to 49% and 29% in the non-halotolerant homologues, respectively. Simulation models showed the DehHX is stable under a highly saline environment (25% w/v) by adopting a highly negative-charged surface with a concomitant weakly interacting hydrophobic core. The study thus, established that a halotolerant dehalogenase undergoes notable evolutionary structural changes related to GC content over its non-halotolerant counterpart, in order to adapt and thrive under highly saline environments. Communicated by Ramaswamy H. Sarma. Taylor and Francis Ltd. 2020-08-12 Article PeerReviewed Edbeib, Mohamed Faraj and Aksoy, Hasan Murat and Kaya, Yilmaz and Abdul Wahab, Roswanira and Huyop, Fahrul (2020) Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases. Journal of Biomolecular Structure and Dynamics, 38 (12). pp. 3452-3461. ISSN 0739-1102 http://dx.doi.org/10.1080/07391102.2019.1657498 DOI:10.1080/07391102.2019.1657498 |
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QD Chemistry Edbeib, Mohamed Faraj Aksoy, Hasan Murat Kaya, Yilmaz Abdul Wahab, Roswanira Huyop, Fahrul Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
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Halophiles are extremophilic microorganisms that grow optimally at high salt concentrations by producing a myriad of equally halotolerant enzymes. Structural haloadaptation of these enzymes adept to thriving under high-salt environments, though are not fully understood. Herein, the study attempts an in silico investigation to identify and comprehend the evolutionary structural adaptation of a halotolerant dehalogenase, DehHX (GenBank accession number: KR297065) of the halotolerant Pseudomonas halophila, over its non-halotolerant counterpart, DehMX1 (GenBank accession number KY129692) produced by Pseudomonas aeruginosa. GC content of the halotolerant DehHX DNA sequence was distinctively higher (58.9%) than the non-halotolerant dehalogenases (55% average GC). Its acidic residues, Asp and Glu were 8.27% and 12.06%, respectively, compared to an average 5.5% Asp and 7% Glu, in the latter; but lower contents of basic and hydrophobic residues in the DehHX. The secondary structure of DehHX interestingly revealed a lower incidence of α-helix forming regions (29%) and a higher percentage of coils (57%), compared to 49% and 29% in the non-halotolerant homologues, respectively. Simulation models showed the DehHX is stable under a highly saline environment (25% w/v) by adopting a highly negative-charged surface with a concomitant weakly interacting hydrophobic core. The study thus, established that a halotolerant dehalogenase undergoes notable evolutionary structural changes related to GC content over its non-halotolerant counterpart, in order to adapt and thrive under highly saline environments. Communicated by Ramaswamy H. Sarma. |
format |
Article |
author |
Edbeib, Mohamed Faraj Aksoy, Hasan Murat Kaya, Yilmaz Abdul Wahab, Roswanira Huyop, Fahrul |
author_facet |
Edbeib, Mohamed Faraj Aksoy, Hasan Murat Kaya, Yilmaz Abdul Wahab, Roswanira Huyop, Fahrul |
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Edbeib, Mohamed Faraj |
title |
Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
title_short |
Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
title_full |
Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
title_fullStr |
Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
title_full_unstemmed |
Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
title_sort |
haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases |
publisher |
Taylor and Francis Ltd. |
publishDate |
2020 |
url |
http://eprints.utm.my/id/eprint/92377/ http://dx.doi.org/10.1080/07391102.2019.1657498 |
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13.160551 |