ArticleSynthetic and systems biotechnology2021
O-glycosyltransferases from
Article in Synthetic and systems biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Yeast species resource exploration and application in cell factories.Synthetic and systems biotechnology · 2026Review
- Discovery and engineering of UDP-glycosyltransferase and its applications in natural sweetener glycosylation.World journal of microbiology & biotechnology · 2026Review
- Advanced applications of synthetic biology technology in biosynthesis of bioactive compounds from medicinal plants.Chinese herbal medicines · 2026Review
- Glycyrrhiza, a commonly used medicinal herb: Review of species classification, pharmacology, active ingredient biosynthesis, and synthetic biology.Journal of advanced research · 2025Review
- Biosynthesis and metabolic engineering of natural sweeteners.AMB Express · 2025Review
- Multi-strategy ugt mining, modification and glycosyl donor synthesis facilitate the production of triterpenoid saponins.Frontiers in plant science · 2025Review
- Recent Advances in the Biosynthesis of Natural Sugar Substitutes in Yeast.Journal of fungi (Basel, Switzerland) · 2023Review
- Glycosyltransferases: Mining, engineering and applications in biosynthesis of glycosylated plant natural products.Synthetic and systems biotechnology · 2022Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycyrrhizin (GL) and Glycyrrhetic Acid 3-O-mono-β-D-glucuronide (GAMG) are the typical triterpenoid glycosides found in the root of licorice, a popular medicinal plant that exhibits diverse physiological effects and pharmacological manifestations. However, only few reports are available on the glycosylation enzymes involved in the biosynthesis of these valuable compounds with low conversion yield so far. In mammals, glycosyltransferases are involved in the phase II metabolism and may provide new solutions for us to engineer microbial strains to produce high valued compounds due to the substrate promiscuity of these glycosyltransferases. In this study, we mined the genomic databases of mammals and evaluated 22 candidate genes of O-glycosyltransferases by analyzing their catalytic potential for O-glycosylation of the native substrate, glycyrrhetinic acid (GA) for its glycodiversification. Out of 22 selected glycosyltransferases, only UGT1A1 exhibited high catalytic performance for biosynthesis of the key licorice compounds GL and GAMG. Molecular docking results proposed that the enzymatic activity of UGT1A1 was likely owing to the stable hydrogen bonding interactions and favorite conformations between the amino acid residues around substrate channels (P82~R85) and substrates. Furthermore, the complete biosynthesis pathway of GL was reconstructed in
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.