ArticleCommunications chemistry2023
Enhancing the thermostability and activity of glycosyltransferase UGT76G1 via computational design.
Article in Communications chemistry, 2023. 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.
- Discovery and engineering of UDP-glycosyltransferase and its applications in natural sweetener glycosylation.World journal of microbiology & biotechnology · 2026Review
- Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026Review
- Protein folding stability estimation with explicit consideration of unfolded states.Nature communications · 2026Article
- Glycoengineering strategies for constructing defined Mucin O-glycans.Frontiers in molecular biosciences · 2026Review
- DDGWizard: Integration of feature calculation resources for analysis and prediction of changes in protein thermostability upon point mutations.PLoS computational biology · 2025Article
- Chemoenzymatic synthesis.Communications chemistry · 2025Article
- Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The diterpene glycosyltransferase UGT76G1, derived from Stevia rebaudiana, plays a pivotal role in the biosynthesis of rebaudioside A, a natural sugar substitute. Nevertheless, its potential for industrial application is limited by certain enzymatic characteristics, notably thermostability. To enhance the thermostability and enzymatic activity, we employed a computational design strategy, merging stabilizing mutation scanning with a Rosetta-based protein design protocol. Compared to UGT76G1, the designed variant 76_4 exhibited a 9 °C increase in apparent T
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Registered trials
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