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Showing 1–11 of 11 results
Advanced filters: Author: Bernd Nidetzky Clear advanced filters

  • Enzymes involve structural flexibility in their function, but understanding enzyme catalysis as connected to protein motions is a major challenge. Here, the authors obtain energetic description of C-H activation in nicotinamide coenzyme-dependent UDP-glucuronic acid C4 epimerase based on temperature kinetic studies and isotope effect measurements.

    • Christian Rapp
    • Annika Borg
    • Bernd Nidetzky
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-10

  • C-nucleosides are analogues of the canonical N-nucleosides and, despite their synthetic value, biocatalysis has not targeted them yet. Here, the authors report a pseudouridine monophosphate C-glycosidase enzyme for selective 5-β-C-glycosylation of uracil and its derivatives from pentose 5- phosphate substrates.

    • Martin Pfeiffer
    • Bernd Nidetzky
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • Pseudouridine (Ψ), the C-nucleoside isomer of uridine, and its 1-N-methyl derivative, are incorporated in mRNA vaccines and essential for their efficiency, but difficult to synthetically access. Here, the authors report on selective and atom-economic 1N-5C rearrangement of β-d-ribosyl on uracil to obtain Ψ from unprotected U in quantitative yield

    • Martin Pfeiffer
    • Andrej Ribar
    • Bernd Nidetzky
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-13

  • Biological degradation of glycosides involves, alongside hydrolysis, β-elimination for glycosidic bond cleavage. Here, the authors report an O-glycoside β-eliminase from Agrobacterium tumefaciens that converts the C3-oxidized O-β-d-glucoside of phloretin into the aglycone and the 2-hydroxy-3-keto-d-glycal elimination product, and suggest convergent evolution of β-eliminase active sites for the cleavage of natural product 3-keto-O-glycosides.

    • Johannes Bitter
    • Martin Pfeiffer
    • Bernd Nidetzky
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Understanding the role of enzymes in biomass depolymerization is essential for the development of more efficient biorefineries. Here, the authors show by atomic force microscopy the real-time mechanism of cellulose deconstruction by lytic polysaccharide monooxygenases.

    • Manuel Eibinger
    • Jürgen Sattelkow
    • Bernd Nidetzky
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-7

  • Biocatalysis needs improved reproducibility and quality of research reporting. Our interdisciplinary team has developed a flexible and extensible metadata catalogue based on STRENDA guidelines, essential for describing complex experimental setups in biocatalysis. The catalogue is available online via GitHub for community use.

    • Stephan Malzacher
    • Dominik Meißner
    • Dörte Rother
    Comments & Opinion
    Nature Catalysis
    Volume: 7, P: 1245-1249

  • Uridine diphosphate-dependent glycosyltransferases (UGTs) play a vital role in the biocatalytic glycosylation of phenolic compounds, however, UGT-catalyzed transformations remain not well-characterized. Here, the authors investigate new members of UGT72 and UGT84 families, revealing their specific reactivity and regio-selectivity on selected polyphenolic substrates.

    • Tuo Li
    • Annika J. E. Borg
    • Bernd Nidetzky
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-12

  • Cellulose chains with a reducing-end thiol group are of interest to install a controllable topochemical pattern of site-selective modification into nanocellulose materials. Selection of the polymerizing enzyme (cellodextrin phosphorylase; CdP) was pursued here to enhance the synthetic precision in the preparation of 1-thio-cellulose. The CdP from Clostridium stercorarium (CsCdP) was identified as a practical catalyst for 1-thio-cellulose synthesis in high purity (≥95%) directly from β-1-thio-glucose. The synthesis proceeds without the need of cellobiose phosphorylase (CbP) and minimizes the contamination (plain cellulose; ≤5%) in the product.

    • Chao Zhong
    • Bernd Nidetzky
    ResearchOpen Access
    Polymer Journal
    Volume: 54, P: 551-560