Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts

Moulis, Claire; Guieysse, David; Morel, Sandrine; Séverac, Etienne; Remaud‐Siméon, Magali

doi:10.1016/j.cbpa.2020.11.004

Cited by 26 publications

(22 citation statements)

References 83 publications

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“…The glycosylated molecules demonstrated more advantages than the original aglycone molecules. After glycosylation, the aqueous solubility of the glycosylated derivatives was greatly increased [ 18 , 19 ]. Accordingly, the aqueous solubility of GAG and the two GAG saponins are listed in Table 2 .…”

Section: Resultsmentioning

confidence: 99%

Glycosylation of Ganoderic Acid G by Bacillus Glycosyltransferases

Ding

Wang

et al. 2021

IJMS

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Ganoderma lucidum is a medicinal fungus abundant in triterpenoids, its primary bioactive components. Although numerous Ganoderma triterpenoids have already been identified, rare Ganoderma triterpenoid saponins were recently discovered. To create novel Ganoderma saponins, ganoderic acid G (GAG) was selected for biotransformation using four Bacillus glycosyltransferases (GTs) including BtGT_16345 from the Bacillus thuringiensis GA A07 strain and three GTs (BsGT110, BsUGT398, and BsUGT489) from the Bacillus subtilis ATCC 6633 strain. The results showed that BsUGT489 catalyzed the glycosylation of GAG to GAG-3-o-β-glucoside, while BsGT110 catalyzed the glycosylation of GAG to GAG-26-o-β-glucoside, which showed 54-fold and 97-fold greater aqueous solubility than that of GAG, respectively. To our knowledge, these two GAG saponins are new compounds. The glycosylation specificity of the four Bacillus GTs highlights the possibility of novel Ganoderma triterpenoid saponin production in the future.

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Section: Resultsmentioning

confidence: 99%

Glycosylation of Ganoderic Acid G by Bacillus Glycosyltransferases

Ding

Wang

et al. 2021

IJMS

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“…Two types of enzymes have been shown to glycosylate such molecules: Leloir glycosyltransferases (GTs) [14,15] and some glycoside hydrolases (GHs) [16,17]. According to the carbohydrate-activating enzyme (CAZy) database, 114 GT families and 117 GH families have been discovered to date.…”

Section: Glycosylation Of Vitexin By Ghs and Gtsmentioning

confidence: 99%

“…Given the dearth of studies on the glycosylation of vitexin and the need to further examine vitexin, the enzymatic glycosylation of vitexin was investigated as a case study. Two types of enzymes have been shown to glycosylate such molecules: Leloir glycosyltransferases (GTs) [14,15] and some glycoside hydrolases (GHs) [16,17]. According to the carbohydrate-activating enzyme (CAZy) database, 114 GT families and 117 GH families have been discovered to date.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Synthesis of Novel Vitexin Glucosides

Wang

Ding

et al. 2021

Molecules

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Vitexin is a C-glucoside flavone that exhibits a wide range of pharmaceutical activities. However, the poor solubility of vitexin limits its applications. To resolve this limitation, two glycoside hydrolases (GHs) and four glycosyltransferases (GTs) were assayed for glycosylation activity toward vitexin. The results showed that BtGT_16345 from the Bacillus thuringiensis GA A07 strain possessed the highest glycosylation activity, catalyzing the conversion of vitexin into new compounds, vitexin-4′-O-β-glucoside (1) and vitexin-5-O-β-glucoside (2), which showed greater aqueous solubility than vitexin. To our knowledge, this is the first report of vitexin glycosylation. Based on the multiple bioactivities of vitexin, the two highly soluble vitexin derivatives might have high potential for pharmacological usage in the future.

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“…In transglycosylases, oligo-or polysaccharide acceptors react instead of water, resulting in a new glycosidic bond. Therefore, transglycosylases are attractive tools for developing a variety of glycoproducts [4], including oligosaccharides and glycoconjugates with applications in food, pharma, and other industries. Some examples with main specificities for α-glucosyl groups, include cyclomaltodextrin glucanotransferases (CGTases in family GH13) [5,6].…”

Section: Introductionmentioning

confidence: 99%

Modeled 3D-Structures of Proteobacterial Transglycosylases from Glycoside Hydrolase Family 17 Give Insight in Ligand Interactions Explaining Differences in Transglycosylation Products

et al. 2021

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The structures of glycoside hydrolase family 17 (GH17) catalytic modules from modular proteins in the ndvB loci in Pseudomonas aeruginosa (Glt1), P. putida (Glt3) and Bradyrhizobium diazoefficiens (previously B. japonicum) (Glt20) were modeled to shed light on reported differences between these homologous transglycosylases concerning substrate size, preferred cleavage site (from reducing end (Glt20: DP2 product) or non-reducing end (Glt1, Glt3: DP4 products)), branching (Glt20) and linkage formed (1,3-linkage in Glt1, Glt3 and 1,6-linkage in Glt20). Hybrid models were built and stability of the resulting TIM-barrel structures was supported by molecular dynamics simulations. Catalytic amino acids were identified by superimposition of GH17 structures, and function was verified by mutagenesis using Glt20 as template (i.e., E120 and E209). Ligand docking revealed six putative subsites (−4, −3, −2, −1, +1 and +2), and the conserved interacting residues suggest substrate binding in the same orientation in all three transglycosylases, despite release of the donor oligosaccharide product from either the reducing (Glt20) or non-reducing end (Glt1, Gl3). Subsites +1 and +2 are most conserved and the difference in release is likely due to changes in loop structures, leading to loss of hydrogen bonds in Glt20. Substrate docking in Glt20 indicate that presence of covalently bound donor in glycone subsites −4 to −1 creates space to accommodate acceptor oligosaccharide in alternative subsites in the catalytic cleft, promoting a branching point and formation of a 1,6-linkage. The minimum donor size of DP5, can be explained assuming preferred binding of DP4 substrates in subsite −4 to −1, preventing catalysis.

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Natural and engineered transglycosylases: Green tools for the enzyme-based synthesis of glycoproducts

Cited by 26 publications

References 83 publications

Glycosylation of Ganoderic Acid G by Bacillus Glycosyltransferases

Glycosylation of Ganoderic Acid G by Bacillus Glycosyltransferases

Enzymatic Synthesis of Novel Vitexin Glucosides

Modeled 3D-Structures of Proteobacterial Transglycosylases from Glycoside Hydrolase Family 17 Give Insight in Ligand Interactions Explaining Differences in Transglycosylation Products

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