ArticleMicrobial biotechnology2019
Phylogeny-guided characterization of glycosyltransferases for epothilone glycosylation.
Article in Microbial biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Review
- Unnatural activities and mechanistic insights of cytochrome P450 PikC gained from site-specific mutagenesis by non-canonical amino acids.Nature communications · 2023Article
- Evaluation of double expression system for co-expression and co-immobilization of flavonoid glucosylation cascade.Applied microbiology and biotechnology · 2022Article
- Impact of novel microbial secondary metabolites on the pharma industry.Applied microbiology and biotechnology · 2022Review
- Docking-guided rational engineering of a macrolide glycosyltransferase glycodiversifies epothilone B.Communications biology · 2022Article
- Midecamycin Is Inactivated by Several Different Sugar Moieties at Its Inactivation Site.International journal of molecular sciences · 2021Article
- Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.Computational and structural biotechnology journal · 2020Review
- Phylogeny-guided characterization of glycosyltransferases for epothilone glycosylation.Microbial biotechnology · 2019Article
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11 authors.
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Abstract
Glycosylation of natural products can influence their pharmacological properties, and efficient glycosyltransferases (GTs) are critical for this purpose. The polyketide epothilones are potent anti-tumour compounds, and YjiC is the only reported GT for the glycosylation of epothilone. In this study, we phylogenetically analysed 8261 GTs deposited in CAZy database and revealed that YjiC locates in a subbranch of the Macrolide I group, forming the YjiC-subbranch with 160 GT sequences. We demonstrated that the YjiC-subbranch GTs are normally efficient in epothilone glycosylation, but some showed low glycosylation activities. Sequence alignment of YjiC-subbranch showed that the 66th and 77th amino acid residues, which were close to the catalytic cavity in molecular docking model, were conserved in five high-active GTs (Q66 and P77) but changed in two low-efficient GTs. Site-directed residues swapping at the two positions in the two low-active GTs (BssGT and BamGT) and the high-active GT BsGT-1 demonstrated that the two amino acid residues played an important role in the catalytic efficiency of epothilone glycosylation. This study highlights that the potent GTs for appointed compounds are phylogenetically grouped with conserved residues for the catalytic efficiency.
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