8hok
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hok OCA], [https://pdbe.org/8hok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hok RCSB], [https://www.ebi.ac.uk/pdbsum/8hok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hok ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8hok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hok OCA], [https://pdbe.org/8hok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hok RCSB], [https://www.ebi.ac.uk/pdbsum/8hok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hok ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glycosylation is an important post-modification reaction in plant secondary metabolism, and contributes to structural diversity of bioactive natural products. In plants, glycosylation is usually catalyzed by UDP-glycosyltransferases. Flavonoid 2'-O-glycosides are rare glycosides. However, no UGTs have been reported, thus far, to specifically catalyze 2'-O-glycosylation of flavonoids. In this work, UGT71AP2 was identified from the medicinal plant Scutellaria baicalensis as the first flavonoid 2'-O-glycosyltransferase. It could preferentially transfer a glycosyl moiety to 2'-hydroxy of at least nine flavonoids to yield six new compounds. Some of the 2'-O-glycosides showed noticeable inhibitory activities against cyclooxygenase 2. The crystal structure of UGT71AP2 (2.15 A) was solved, and mechanisms of its regio-selectivity was interpreted by pK (a) calculations, molecular docking, MD simulation, MM/GBSA binding free energy, QM/MM, and hydrogenâdeuterium exchange mass spectrometry analysis. Through structure-guided rational design, we obtained the L138T/V179D/M180T mutant with remarkably enhanced regio-selectivity (the ratio of 7-O-glycosylation byproducts decreased from 48% to 4%) and catalytic efficiency of 2'-O-glycosylation (k (cat)/K (m), 0.23 L/(s.mumol), 12-fold higher than the native). Moreover, UGT71AP2 also possesses moderate UDP-dependent de-glycosylation activity, and is a dual function glycosyltransferase. This work provides an efficient biocatalyst and sets a good example for protein engineering to optimize enzyme catalytic features through rational design. | ||
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| + | Functional characterization, structural basis, and protein engineering of a rare flavonoid 2'-O-glycosyltransferase from Scutellaria baicalensis.,Wang Z, Du X, Ye G, Wang H, Liu Y, Liu C, Li F, Agren H, Zhou Y, Li J, He C, Guo DA, Ye M Acta Pharm Sin B. 2024 Aug;14(8):3746-3759. doi: 10.1016/j.apsb.2024.04.001. Epub , 2024 Apr 5. PMID:39220864<ref>PMID:39220864</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8hok" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
crystal structure of UGT71AP2
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Categories: Large Structures | Scutellaria baicalensis | He C | Li F | Qiao X | Wang ZL | Ye M
