Regioselective glycosylation is a chemical challenge, leading to multistep syntheses with protecting group manipulations, ultimately resulting in poor atom economy and compromised sustainability. Enzymes allow eco-friendly and regioselective bond formation with fully deprotected substrates in a single reaction. For the selective glucosylation of silibinin, a pharmaceutical challenged with low solubility, enzyme engineering has previously been employed, but the resulting yields and were limited, prohibiting the application of the engineered catalyst. Here, we identified a naturally regioselective silibinin glucosyltransferase, UGT706F8, a family 1 glycosyltransferase from . It selectively and efficiently ( = 2.1 ± 0.1 s; = 36.9 ± 5.2 μM; TTN = 768 ± 22) catalyzes the quantitative synthesis of silibinin 7--β-d-glucoside. We solved the crystal structure of UGT706F8 and investigated the molecular determinants of regioselective silibinin glucosylation. UGT706F8 was the only regioselective enzyme among 18 glycosyltransferases found to be active on silibinin. We found the temperature optimum of UGT706F8 to be 34 °C and the pH optimum to be 7-8. Our results indicate that UGT706F8 is an efficient silibinin glycosyltransferase that enables biocatalytic production of silbinin 7--β-d-glucoside.
Glycosylation is one of the most fundamental biochemical processes in cells. It plays crucial roles in diversifying plant natural products for structures, bioavailability and bioactivity, and thus, renders the glycosylated compounds valuable as food additives, nutraceuticals and pharmaceuticals. Moreover, glycosylated compounds impact plant growth, development and stress response.
Having alternative infection routes is thought to help parasites circumvent host resistance, provided that these routes are associated with different host resistance loci. This study tests this postulate by examining whether alternate infection routes of the parasite Pasteuria ramosa are linked to distinct resistance loci in its crustacean host, Daphnia magna. We focus on the P.
Analytical and Testing Center, Anhui Dabieshan Chinese Medicine Research Institute, Anhui Engineering Research Center for Eco-agriculture of Traditional Chinese Medicine, West Anhui University Lu'an 237012, China.
UDP-rhamnose, which is synthesized under the catalysis by the rhamnose synthase(RHM), is an essential sugar donor for the synthesis of rhamnoside in plants. Based on the reported rhamnose synthase, this study screened one RHM gene(DhuRHM) from the localized gene database of Dendrobium huoshanense by sequence alignment. This gene was cloned, and then bioinformatics analysis and in vitro functional verification were carried out.
UDP-glycosyltransferases (UGTs) widely exist in plants and play essential roles in catalyzing the glycosylation reaction associated with metabolic processes. UGT gene family has been identified in many species to date. However, the comprehensive identification and systematic analysis have not been documented yet in the latest potato genome.
Polypeptide N-acetylgalactosaminyltransferase-like protein 5 (GALNTL5) was identified as a pp-GalNAc-T family gene. Nevertheless, GALNTL5 has no glycosyltransferase activity. In mice, Galntl5 expression is restricted to differentiating spermatids, and haploinsufficiency leads to immotile spermatozoa with an aberrant protein composition.
