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Glycolipid glycosyltransferase with broad substrate specificity from the marine bacterium “Candidatus Pelagibacter sp.” Strain HTCC7211
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Wei, Tao, Zhao, Caimeng, Quareshy, Mussa, Wu, Nan, Huang, Shen, Zhao, Yuezhe, Yang, Pengfei, Mao, Duobin and Chen, Yin (2021) Glycolipid glycosyltransferase with broad substrate specificity from the marine bacterium “Candidatus Pelagibacter sp.” Strain HTCC7211. Applied and Environmental Microbiology, 87 (14). e00326-21. doi:10.1128/AEM.00326-21 ISSN 0099-2240.
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Official URL: https://doi.org/10.1128/AEM.00326-21
Abstract
In the marine environment, phosphorus availability significantly affects the lipid composition in many cosmopolitan marine heterotrophic bacteria, including members of the SAR11 clade and the Roseobacter clade. Under phosphorus stress conditions, nonphosphorus sugar-containing glycoglycerolipids are substitutes for phospholipids in these bacteria. Although these glycoglycerolipids play an important role as surrogates for phospholipids under phosphate deprivation, glycoglycerolipid synthases in marine microbes are poorly studied. In the present study, we biochemically characterized a glycolipid glycosyltransferase (GTcp) from the marine bacterium “Candidatus Pelagibacter sp.” strain HTCC7211, a member of the SAR11 clade. Our results showed that GTcp is able to act as a multifunctional enzyme by synthesizing different glycoglycerolipids with UDP-glucose, UDP-galactose, or UDP-glucuronic acid as sugar donors and diacylglycerol (DAG) as the acceptor. Analyses of enzyme kinetic parameters demonstrated that Mg2+ notably changes the enzyme’s affinity for UDP-glucose, which improves its catalytic efficiency. Homology modeling and mutational analyses revealed binding sites for the sugar donor and the diacylglycerol lipid acceptor, which provided insights into the retaining mechanism of GTcp with its GT-B fold. A phylogenetic analysis showed that GTcp and its homologs form a group in the GT4 glycosyltransferase family. These results not only provide new insights into the glycoglycerolipid synthesis mechanism in lipid remodeling but also describe an efficient enzymatic tool for the future synthesis of bioactive molecules.
Item Type: | Journal Article | ||||||||||||
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Subjects: | Q Science > QP Physiology Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||
Library of Congress Subject Headings (LCSH): | Marine bacteria, Glycosyltransferases, Glycosyltransferase genes, Phospholipids, Glycolipids, Marine microbial ecology | ||||||||||||
Journal or Publication Title: | Applied and Environmental Microbiology | ||||||||||||
Publisher: | American Society for Microbiology | ||||||||||||
ISSN: | 0099-2240 | ||||||||||||
Official Date: | 25 June 2021 | ||||||||||||
Dates: |
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Volume: | 87 | ||||||||||||
Number: | 14 | ||||||||||||
Article Number: | e00326-21 | ||||||||||||
DOI: | 10.1128/AEM.00326-21 | ||||||||||||
Status: | Peer Reviewed | ||||||||||||
Publication Status: | Published | ||||||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||
Copyright Holders: | Copyright © 2021 Wei et al. | ||||||||||||
Date of first compliant deposit: | 21 April 2021 | ||||||||||||
Date of first compliant Open Access: | 21 May 2021 | ||||||||||||
RIOXX Funder/Project Grant: |
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