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    Synthesis and effect of nonhydrolyzable xanthosine triphosphate derivatives on prenylation of Rab5D136N

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    Authors
    Yanachkov, Ivan
    Pan, Julie Y.
    Wessling-Resnick, Marianne
    Wright, George E.
    UMass Chan Affiliations
    Department of Pharmacology and Molecular Toxicology
    Document Type
    Journal Article
    Publication Date
    1997-01-01
    Keywords
    GTP Phosphohydrolases
    GTP-Binding Proteins
    Hydrolysis
    Protein Prenylation
    Ribonucleotides
    rab5 GTP-Binding Proteins
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    https://doi.org/10.1124/mol.51.1.47
    Abstract
    A novel and convenient method for nucleoside triphosphate synthesis was applied to the preparation of potentially nonhydrolyzable xanthosine triphosphate derivatives. The N-methylimidazolide of xanthosine 5'-monophosphate reacted rapidly with methylenediphosphonic acid and imidodiphosphonic acid to give xanthosine 5'-(beta, gamma-methylene)triphosphate and xanthosine 5'-(beta, gamma-imido)triphosphate, respectively, in good yields. Both compounds inhibited the xanthosine-diphosphate-dependent prenylation of a mutant of Rab5, Rab5D136N, the nucleotide specificity of which had been converted from GTP to xanthosine triphosphate. The results indicate that xanthosine 5'-(beta, gamma-methylene)triphosphate and xanthosine 5'-(beta, gamma-imido)triphosphate bound to the mutant protein with similar affinities and were not hydrolyzed under the assay conditions. These novel derivatives may be useful tools for the study of the role of individual GTPases mutated to xanthosine triphosphate specificity in the background of other GTP-binding proteins.
    Source

    Mol Pharmacol. 1997 Jan;51(1):47-51.

    DOI
    10.1124/mol.51.1.47
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38611
    PubMed ID
    9016345
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1124/mol.51.1.47
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