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Condensation reactions catalyzed by ?-N-acetylgalactosaminidase from Aspergillus niger yielding a-N-acetylgalactosaminides

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00340836" target="_blank" >RIV/61388971:_____/10:00340836 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Condensation reactions catalyzed by ?-N-acetylgalactosaminidase from Aspergillus niger yielding a-N-acetylgalactosaminides

  • Original language description

    Extracellular a-N-acetylgalactosaminidase from Aspergillus niger catalyzed glycosylation yielding a series of 2-acetamido-2-deoxy-a-D-galactobiosides using 2-acetamido-2-deoxy-D-galactopyranose as a glycosyl donor. The isomers a-D-GalpNAc-D-GalpNAc, a-D-GalpNAc-D-GalpNAc and a-D-GalpNAc-D-GalfNAc were isolated and spectrally characterized. The purified enzyme was further used for the glycosylation of free amino acids (serine and threonine) and their N-(tert-butoxycarbonyl)-protected analogs to synthesize the Tn antigen (GalpNAc-a-O-Ser/Thr) and its N-(tertbutoxycarbonyl)-protected derivatives

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/OC%20136" target="_blank" >OC 136: Combined chemical and enzymatic synthesis of complex multivalent glycoconjungates - ways to new materials and glycodrugs</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2010

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biocatalysis and Biotransformation

  • ISSN

    1024-2422

  • e-ISSN

  • Volume of the periodical

    28

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    6

  • Pages from-to

  • UT code for WoS article

    000274855300008

  • EID of the result in the Scopus database