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Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis.
Coenzyme Q(10) (CoQ(10)) is a powerful antioxidant with a myriad of applications in healthcare and cosmetic industries. The most effective route of CoQ(10) production is microbial biosynthesis. In this study, four CoQ(10) biosynthesizing purple photosynthetic bacteria: Rhodobacter blasticus, Rhodovu...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9672418/ https://www.ncbi.nlm.nih.gov/pubmed/36404947 http://dx.doi.org/10.1016/j.btre.2022.e00775 |
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author | George, Drishya M. Ramadoss, Ramya Mackey, Hamish R. Vincent, Annette S. |
author_facet | George, Drishya M. Ramadoss, Ramya Mackey, Hamish R. Vincent, Annette S. |
author_sort | George, Drishya M. |
collection | PubMed |
description | Coenzyme Q(10) (CoQ(10)) is a powerful antioxidant with a myriad of applications in healthcare and cosmetic industries. The most effective route of CoQ(10) production is microbial biosynthesis. In this study, four CoQ(10) biosynthesizing purple photosynthetic bacteria: Rhodobacter blasticus, Rhodovulum adriaticum, Afifella pfennigii and Rhodovulum marinum, were identified using 16S rRNA sequencing of enriched microbial mat samples obtained from Purple Island mangroves (Qatar). The membrane bound enzyme 4-hydroxybenzoate octaprenyltransferase (UbiA) is pivotal for bacterial biosynthesis of CoQ(10). The identified bacteria could be inducted as efficient industrial bio-synthesizers of CoQ(10) by engineering their UbiA enzymes. Therefore, the mutation sites and substitution residues for potential functional enhancement were determined by comparative computational study. Two mutation sites were identified within the two conserved Asp-rich motifs, and the effect of proposed mutations in substrate binding affinity of the UbiA enzymes was assessed using multiple ligand simultaneous docking (MLSD) studies, as a groundwork for experimental studies. |
format | Online Article Text |
id | pubmed-9672418 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-96724182022-11-19 Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. George, Drishya M. Ramadoss, Ramya Mackey, Hamish R. Vincent, Annette S. Biotechnol Rep (Amst) Research Article Coenzyme Q(10) (CoQ(10)) is a powerful antioxidant with a myriad of applications in healthcare and cosmetic industries. The most effective route of CoQ(10) production is microbial biosynthesis. In this study, four CoQ(10) biosynthesizing purple photosynthetic bacteria: Rhodobacter blasticus, Rhodovulum adriaticum, Afifella pfennigii and Rhodovulum marinum, were identified using 16S rRNA sequencing of enriched microbial mat samples obtained from Purple Island mangroves (Qatar). The membrane bound enzyme 4-hydroxybenzoate octaprenyltransferase (UbiA) is pivotal for bacterial biosynthesis of CoQ(10). The identified bacteria could be inducted as efficient industrial bio-synthesizers of CoQ(10) by engineering their UbiA enzymes. Therefore, the mutation sites and substitution residues for potential functional enhancement were determined by comparative computational study. Two mutation sites were identified within the two conserved Asp-rich motifs, and the effect of proposed mutations in substrate binding affinity of the UbiA enzymes was assessed using multiple ligand simultaneous docking (MLSD) studies, as a groundwork for experimental studies. Elsevier 2022-11-12 /pmc/articles/PMC9672418/ /pubmed/36404947 http://dx.doi.org/10.1016/j.btre.2022.e00775 Text en © 2022 The Authors. Published by Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article George, Drishya M. Ramadoss, Ramya Mackey, Hamish R. Vincent, Annette S. Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. |
title | Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. |
title_full | Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. |
title_fullStr | Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. |
title_full_unstemmed | Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. |
title_short | Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q(10) biosynthesis. |
title_sort | comparative computational study to augment ubia prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in qatar for coenzyme q(10) biosynthesis. |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9672418/ https://www.ncbi.nlm.nih.gov/pubmed/36404947 http://dx.doi.org/10.1016/j.btre.2022.e00775 |
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