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Structure-function relationships in NDP-sugar active SDR enzymes: Fingerprints for functional annotation and enzyme
Matthieu Da Costa1, Ophelia Gevaert1, Stevie Van Overtveldt1
1Centre for Synthetic Biology - Unit for Biocatalysis and Enzyme Engineering, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, 9000 Gent, Belgium.
This review analyzes Short-chain Dehydrogenase/Reductase enzymes (NS-SDR) involved in rare sugar biosynthesis. A new "heptagonal box model" is proposed, offering specificity fingerprints for enzyme annotation and engineering.
Area of Science:
- Biochemistry
- Enzymology
- Carbohydrate Chemistry
Background:
- Short-chain Dehydrogenase/Reductase enzymes active on nucleotide sugars (NS-SDR) are crucial for synthesizing rare sugars and glycosides.
- Specific NS-SDR family members are linked to metabolic disorders and virulence factor production.
- Existing research often focuses on individual NS-SDR activities, limiting a comprehensive understanding.
Purpose of the Study:
- To provide an in-depth overview of all NS-SDR families by integrating knowledge from diverse studies.
- To identify conserved patterns and crucial residues across 169,076 NS-SDR enzyme sequences.
- To propose an updated specificity model for NS-SDR enzymes.
Main Methods:
- Structure-based multiple sequence alignment of NS-SDR enzymes from public databases.
- Analysis of conserved residues and their correlation with enzyme function.
- Comparison with existing models, such as the UDP-galactose 4-epimerase hexagonal box model.
Main Results:
- Identification of clear conservation patterns and correlations among crucial residues in NS-SDRs.
- Proposal of an updated
Conclusions:
- The proposed
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