Near-perfect control of the regioselective glucosylation enabled by rational design of glycosyltransferases - ScienceDirect
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Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
![](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41467-019-11154-4/MediaObjects/41467_2019_11154_Fig5_HTML.png)
Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
![](https://ars.els-cdn.com/content/image/1-s2.0-S2667370323000668-gr1.jpg)
Rational design of a highly active N-glycosyltransferase mutant using fragment replacement approach - ScienceDirect
![](https://ars.els-cdn.com/content/image/1-s2.0-S0926669022012675-gr3.jpg)
Structurefunction relationships in plant UDP-glycosyltransferases - ScienceDirect
![](https://ars.els-cdn.com/content/image/1-s2.0-S2666554921000053-gr3.jpg)
Near-perfect control of the regioselective glucosylation enabled by rational design of glycosyltransferases - ScienceDirect
![](https://ars.els-cdn.com/content/image/1-s2.0-S0141813024004811-gr3.jpg)
Evolving the 3-O/6-O regiospecificity of a microbial glycosyltransferase for efficient production of ginsenoside Rh1 and unnatural ginsenoside - ScienceDirect
![](https://ars.els-cdn.com/content/image/1-s2.0-S0141813024004811-gr4.jpg)
Evolving the 3-O/6-O regiospecificity of a microbial glycosyltransferase for efficient production of ginsenoside Rh1 and unnatural ginsenoside - ScienceDirect
![](https://i1.rgstatic.net/publication/349333015_Disaccharide_phosphorylases_Structure_catalytic_mechanisms_and_directed_evolution/links/6043af2c299bf1e0785f4d23/largepreview.png)
PDF) Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution
![](https://www.frontiersin.org/files/Articles/540883/fchem-08-00645-HTML/image_m/fchem-08-00645-g003.jpg)
Frontiers Cell-Free Synthetic Glycobiology: Designing and Engineering Glycomolecules Outside of Living Cells
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Utilization of glycosyltransferases as a seamless tool for synthesis and modification of the oligosaccharides-A review - ScienceDirect
![](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41467-019-11154-4/MediaObjects/41467_2019_11154_Fig4_HTML.png)
Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
![](https://ars.els-cdn.com/content/image/1-s2.0-S0141813024004811-ga1.jpg)
Evolving the 3-O/6-O regiospecificity of a microbial glycosyltransferase for efficient production of ginsenoside Rh1 and unnatural ginsenoside - ScienceDirect
![](https://ars.els-cdn.com/content/image/1-s2.0-S0734975023000538-gr1.jpg)
Engineered production of bioactive polyphenolic O-glycosides - ScienceDirect
![](https://www.researchgate.net/publication/349333015/figure/fig3/AS:998401260941313@1615048818709/The-distribution-of-efforts-made-on-DSPs-engineering-SP-sucrose-phosphorylase-CBP_Q320.jpg)
PDF) Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution
![](https://ars.els-cdn.com/content/image/1-s2.0-S2468823123008374-gr10.jpg)
Focused rational iterative site-specific mutagenesis (FRISM): A powerful method for enzyme engineering - ScienceDirect