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Tytuł:
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Structure-function relationships in NDP-sugar active SDR enzymes: Fingerprints for functional annotation and enzyme engineering.
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Autorzy:
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Da Costa M; Centre for Synthetic Biology - Unit for Biocatalysis and Enzyme Engineering, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, 9000 Gent, Belgium.
Gevaert O; Centre for Synthetic Biology - Unit for Biocatalysis and Enzyme Engineering, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, 9000 Gent, Belgium.
Van Overtveldt S; Centre for Synthetic Biology - Unit for Biocatalysis and Enzyme Engineering, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, 9000 Gent, Belgium.
Lange J; Bio-Prodict BV, Nieuwe Marktstraat 54E, 6511, AA, Nijmegen, the Netherlands.
Joosten HJ; Bio-Prodict BV, Nieuwe Marktstraat 54E, 6511, AA, Nijmegen, the Netherlands.
Desmet T; Centre for Synthetic Biology - Unit for Biocatalysis and Enzyme Engineering, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, 9000 Gent, Belgium. Electronic address: .
Beerens K; Centre for Synthetic Biology - Unit for Biocatalysis and Enzyme Engineering, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, 9000 Gent, Belgium. Electronic address: .
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Źródło:
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Biotechnology advances [Biotechnol Adv] 2021 May-Jun; Vol. 48, pp. 107705. Date of Electronic Publication: 2021 Feb 08.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't; Review
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Język:
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English
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Imprint Name(s):
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Publication: Oxford : Elsevier Science
Original Publication: Oxford ; New York : Pergamon Press, c1983-
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MeSH Terms:
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Oxidoreductases*
Sugars*
Humans ; Sequence Alignment ; Structure-Activity Relationship ; Substrate Specificity
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Contributed Indexing:
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Keywords: Decarboxylase; Dehydratase; Epimerase; NDP-sugars; Reductase; SDR superfamily; Short-chain dehydrogenase/reductase; Specificity fingerprints; Structure-function relationship
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Substance Nomenclature:
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0 (Sugars)
EC 1.- (Oxidoreductases)
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Entry Date(s):
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Date Created: 20210211 Date Completed: 20210428 Latest Revision: 20220531
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Update Code:
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20240104
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DOI:
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10.1016/j.biotechadv.2021.107705
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PMID:
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33571638
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Short-chain Dehydrogenase/Reductase enzymes that are active on nucleotide sugars (abbreviated as NS-SDR) are of paramount importance in the biosynthesis of rare sugars and glycosides. Some family members have already been extensively characterized due to their direct implication in metabolic disorders or in the biosynthesis of virulence factors. In this review, we combine the knowledge gathered from studies that typically focused only on one NS-SDR activity with an in-depth analysis and overview of all of the different NS-SDR families (169,076 enzyme sequences). Through this structure-based multiple sequence alignment of NS-SDRs retrieved from public databases, we could identify clear patterns in conservation and correlation of crucial residues. Supported by this analysis, we suggest updating and extending the UDP-galactose 4-epimerase "hexagonal box model" to an "heptagonal box model" for all NS-SDR enzymes. This specificity model consists of seven conserved regions surrounding the NDP-sugar substrate that serve as fingerprint for each specificity. The specificity fingerprints highlighted in this review will be beneficial for functional annotation of the large group of NS-SDR enzymes and form a guide for future enzyme engineering efforts focused on the biosynthesis of rare and specialty carbohydrates.
(Copyright © 2021 Elsevier Inc. All rights reserved.)
