Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 biosynthesis.

Coenzyme Q10 (CoQ10) is a powerful antioxidant with a myriad of applications in healthcare and cosmetic industries. The most effective route of CoQ10 production is microbial biosynthesis. In this study, four CoQ10 biosynthesizing purple photosynthetic bacteria: Rhodobacter blasticus, Rhodovulum adri...

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Main Authors: Drishya M. George, Ramya Ramadoss, Hamish R. Mackey, Annette S. Vincent
Format: Article
Language:English
Published: Elsevier 2022-12-01
Series:Biotechnology Reports
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2215017X2200073X
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author Drishya M. George
Ramya Ramadoss
Hamish R. Mackey
Annette S. Vincent
author_facet Drishya M. George
Ramya Ramadoss
Hamish R. Mackey
Annette S. Vincent
author_sort Drishya M. George
collection DOAJ
description Coenzyme Q10 (CoQ10) is a powerful antioxidant with a myriad of applications in healthcare and cosmetic industries. The most effective route of CoQ10 production is microbial biosynthesis. In this study, four CoQ10 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 CoQ10. The identified bacteria could be inducted as efficient industrial bio-synthesizers of CoQ10 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.
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spelling doaj.art-770b3c33cd124479bf452ee3500b43e02022-12-22T02:49:48ZengElsevierBiotechnology Reports2215-017X2022-12-0136e00775Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 biosynthesis.Drishya M. George0Ramya Ramadoss1Hamish R. Mackey2Annette S. Vincent3College of Health and Life Sciences, Hamad bin Khalifa University, Qatar Foundation, Doha, QatarBiological Sciences, Carnegie Mellon University Qatar, Doha, QatarCollege of Health and Life Sciences, Hamad bin Khalifa University, Qatar Foundation, Doha, Qatar; Division of Sustainable Development, College of Science and Engineering, Hamad bin Khalifa University, Qatar Foundation, Doha, QatarBiological Sciences, Carnegie Mellon University Qatar, Doha, Qatar; Corresponding author.Coenzyme Q10 (CoQ10) is a powerful antioxidant with a myriad of applications in healthcare and cosmetic industries. The most effective route of CoQ10 production is microbial biosynthesis. In this study, four CoQ10 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 CoQ10. The identified bacteria could be inducted as efficient industrial bio-synthesizers of CoQ10 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.http://www.sciencedirect.com/science/article/pii/S2215017X2200073XAnoxygenic phototrophic bacteria (APB)Resource recoveryPurple photosynthetic bacteria (PPB)Coenzyme Q10 (CoQ10)Protein modelingMultiple ligand simultaneous docking (MLSD)
spellingShingle Drishya M. George
Ramya Ramadoss
Hamish R. Mackey
Annette S. Vincent
Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 biosynthesis.
Biotechnology Reports
Anoxygenic phototrophic bacteria (APB)
Resource recovery
Purple photosynthetic bacteria (PPB)
Coenzyme Q10 (CoQ10)
Protein modeling
Multiple ligand simultaneous docking (MLSD)
title Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 biosynthesis.
title_full Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 biosynthesis.
title_fullStr Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 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 Q10 biosynthesis.
title_short Comparative computational study to augment UbiA prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in Qatar for coenzyme Q10 biosynthesis.
title_sort comparative computational study to augment ubia prenyltransferases inherent in purple photosynthetic bacteria cultured from mangrove microbial mats in qatar for coenzyme q10 biosynthesis
topic Anoxygenic phototrophic bacteria (APB)
Resource recovery
Purple photosynthetic bacteria (PPB)
Coenzyme Q10 (CoQ10)
Protein modeling
Multiple ligand simultaneous docking (MLSD)
url http://www.sciencedirect.com/science/article/pii/S2215017X2200073X
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