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Updated: Jan 6, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Pyruvate Substitutions on Glycoconjugates.
Fiona F Hager1, Leander Sützl2, Cordula Stefanović3
1Department of NanoBiotechnology, NanoGlycobiology unit, Universität für Bodenkultur Wien, Muthgasse 11, A-1190 Vienna, Austria. fiona.hager@boku.ac.at.
Ketal-pyruvylation modifies glycoconjugates in bacteria, algae, and yeast, but not humans. This review explores these widespread modifications, their functions, and the enzymes responsible.
Area of Science:
- Biochemistry
- Glycobiology
- Microbiology
Background:
- Glycoconjugates are diverse biomolecules, often cell-surface located, mediating crucial functions.
- Pyruvylation, a modification of monosaccharides, occurs in enol or ketal forms.
- Ketal-pyruvylation is found in bacteria, algae, and yeast, but notably absent in humans.
Purpose of the Study:
- To review the current knowledge on widespread but under-investigated ketal-pyruvylation.
- To explore the diverse classes of pyruvylated glycoconjugates and their functions.
- To discuss pyruvyltransferases, their specificity, sequence space, and pyruvate analytics.
Main Methods:
- Mild purification strategies to preserve acid-labile ketal-pyruvyl groups.
- Elucidation of pyruvylated glycan structures.
- Compilation of existing information on pyruvyltransferases and their associated organisms.
Main Results:
- Ketal-pyruvylation is a common modification in various organisms, impacting glycoconjugate structure and function.
- Knowledge regarding pyruvyltransferases, their motifs, and genome sequences remains limited.
- Diverse pyruvylated glycoconjugate structures have been identified.
Conclusions:
- Ketal-pyruvylation represents a significant, yet understudied, area in glycobiology.
- Further research into pyruvyltransferases is crucial for understanding their roles in different organisms.
- Pyruvate analytics and enzyme discovery are key for advancing this field.
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