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Probing glycosyltransferase activities with the Staudinger ligation.

Probing glycosyltransferase activities with the Staudinger ligation. Research Abstract Details 

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  • Probing glycosyltransferase activities with the Staudinger ligation. Abstract Text:

    howard c hangHoward C Hang,chong yuChong Yu,matthew r prattMatthew R Pratt,carolyn r bertozziCarolyn R Bertozzi,

    The development of rapid screening methods for probing glycosyltransferase activities is essential for advancing the field of glycobiology. While assays for specific glycosyltransferases exist, there is no generalizable method that can be applied across the enzyme superfamily. Herein we describe a novel glycosyltransferase assay that exploits their unnatural substrate tolerance and the unique chemical reactivity of the azide. We applied this "azido-ELISA" to the family of polypeptide alpha-N-acetylgalactosaminyltransferases (ppGalNAcTs), all of which were able to transfer N-azidoacetylgalactosamine (GalNAz) from the unnatural nucleotide sugar donor UDP-GalNAz. The azide was detected and quantified by Staudinger ligation with a phosphine probe in a microtiter plate format. This approach should be applicable to any glycosyltransferase or group-transfer enzyme that tolerates unnatural azido substrates.

    Probing glycosyltransferase activities with the Staudinger ligation. Publishing Authors By Initials

    hc hangHC Hang,c yuC Yu,mr prattMR Pratt,cr bertozziCR Bertozzi,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Probing glycosyltransferase activities with the Staudinger ligation. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Journal of the American Chemical Society

    VOLUME: 126

    Page Numbers: 6-7

    Journal Abbreviation: J. Am. Chem. Soc.

    ISSN: 0002-7863

    DAY: 14

    MONTH: Jan

    YEAR: 2004

    Probing glycosyltransferase activities with the Staudinger ligation. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7503056

    Probing glycosyltransferase activities with the Staudinger ligation. Keywords Mesh Terms:

    KEYWORDS: Uridine Diphosphate N-Acetylgalactosamin

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Probing glycosyltransferase activities with the Staudinger ligation. Information

    Substance Name: N-Acetylgalactosaminyltransferases

    Registry Number: EC 2.4.1.-

    Grant and Affiliation Information for Probing glycosyltransferase activities with the Staudinger ligation.

    AFFILIATION: Center for New Directions in Organic Synthesis, Departments of Chemistry and Molecular and Cell Biology, and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM66047

    ACRONYM: GM

    MEDLINETA: J Am Chem Soc

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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