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Structural and Molecular Characterization of Squalene Synthase Belonging to the Marine Thraustochytrid Species Aurantiochytrium limacinum Using Bioinformatics Approach
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0001-9732-4172
Department of Biological Engineering, Chalmers University of Technology, 41296 Gothenberg, Sweden; Bioeconomy Division, EviKrets Biobased Processes Consultants, Lunnavågen 87, 42834 Landvetter, Sweden.ORCID iD: 0000-0001-5934-8720
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0001-7500-2367
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0003-0079-5950
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2022 (English)In: Marine Drugs, E-ISSN 1660-3397, Vol. 20, no 3, article id 180Article in journal (Refereed) Published
Abstract [en]

The marine microorganisms thraustochytrids have been explored for their potential in the production of various bioactive compounds, such as DHA, carotenoids, and squalene. Squalene is a secondary metabolite of the triterpenoid class and is known for its importance in various industrial applications. The bioinformatic analysis for squalene synthase (SQS) gene (the first key enzyme in the tri-terpenoid synthesis pathway), that is prevailing among thraustochytrids, is poorly investigated. In-silico studies combining sequence alignments and bioinformatic tools helped in the preliminary characterization of squalene synthases found in Aurantiochytrium limacinum. The sequence contained highly conserved regions for SQS found among different species indicated the enzyme had all the regions for its functionality. The signal peptide sequence and transmembrane regions were absent, indicating an important aspect of the subcellular localization. Secondary and 3-D models generated using appropriate templates demonstrated the similarities with SQS of the other species. The 3-D model also provided important insights into possible active, binding, phosphorylation, and glycosylation sites.

Place, publisher, year, edition, pages
MDPI, 2022. Vol. 20, no 3, article id 180
Keywords [en]
marine thraustochytrids, Aurantiochytrium, squalene, squalene synthase, bioinformatic analysis
National Category
Biochemistry and Molecular Biology Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-89813DOI: 10.3390/md20030180ISI: 000775119700001PubMedID: 35323479Scopus ID: 2-s2.0-85125868428OAI: oai:DiVA.org:ltu-89813DiVA, id: diva2:1646167
Note

Validerad;2022;Nivå 2;2022-03-21 (johcin);

Funder: Swedish Research Council (FORMAS) and Kempestiftelserna (2020-01028), (JCK-2115 L3)

Available from: 2022-03-21 Created: 2022-03-21 Last updated: 2024-07-04Bibliographically approved

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Vyas, SachinRova, UlrikaChristakopoulos, PaulMatsakas, LeonidasPatel, Alok

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