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Updated: Jun 4, 2026
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Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Glycosyltransferases as biocatalysts
1Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark. monica@crc.dk
Current Opinion in Chemical Biology
|February 22, 2011
Summary
Glycosyltransferases are versatile tools for synthesizing complex carbohydrates and their analogs. Advances in enzyme discovery, engineering, and screening enable large-scale production and diversification of natural products.
Area of Science:
- Biochemistry
- Synthetic Biology
- Enzymology
Background:
- Glycosyltransferases are crucial enzymes in carbohydrate synthesis.
- Their application in preparing oligosaccharides and glycoconjugates is well-established.
- Challenges include enzyme availability and specificity for complex syntheses.
Purpose of the Study:
- To highlight the utility of glycosyltransferases as synthetic tools.
- To discuss advancements enabling large-scale and diverse applications.
- To explore new enzyme discovery and engineering strategies.
Main Methods:
- Utilizing recombinant glycosyltransferases for multi-step synthesis.
- Employing modified donor and acceptor substrates.
- Leveraging genome sequencing and CAZy database for enzyme discovery.
- Applying enzyme mutagenesis, domain swapping, and metabolic engineering.
Main Results:
- High expression levels of recombinant enzymes facilitate mg to multi-gram scale synthesis.
- Enzyme tolerance to modified substrates allows preparation of oligosaccharide analogues.
- New enzyme discoveries expand the toolkit for glycosylation.
- Engineering approaches enhance reaction specificity and product diversification.
Conclusions:
- Glycosyltransferases are powerful and adaptable tools for carbohydrate synthesis.
- Ongoing research in enzyme discovery and engineering continues to expand their synthetic capabilities.
- These enzymes are pivotal for producing natural products, analogues, and glycoconjugates.
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