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Related Experiment Videos

[Yersinia pseudotuberculosis nucleoside-kinase].

Iu A Nemtseva, N A Terent'eva, N F Timchenko

    Zhurnal Mikrobiologii, Epidemiologii I Immunobiologii
    |May 11, 2005
    PubMed
    Summary

    Researchers isolated a thymidine- and uridine-kinase enzyme from Y. pseudotuberculosis. This enzyme efficiently phosphorylates thymidine and uridine, crucial for cellular processes.

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    Effect of thermolabile toxin from Yersinia pseudotuberculosis on functions of innate immunity cells.

    Bulletin of experimental biology and medicine·2014

    Area of Science:

    • Biochemistry
    • Enzymology

    Context:

    • Yersinia pseudotuberculosis is a bacterial pathogen.
    • Nucleoside kinases play vital roles in DNA synthesis and repair.

    Purpose:

    • To isolate and characterize a novel enzyme from Y. pseudotuberculosis.
    • To investigate the substrate specificity and optimal conditions for thymidine and uridine phosphorylation.

    Summary:

    • A thymidine- and uridine-kinase was purified approximately 350-fold from Y. pseudotuberculosis using ammonium sulfate fractionation, ion exchange, and affinity chromatography.
    • The purified enzyme demonstrated optimal activity at pH 8-8.5 and 45°C, requiring MgCl2 and ATP.
    • The enzyme phosphorylated thymidine, uridine, and deoxycytidine but not thymidine monophosphate, indicating broad substrate acceptance.

    Impact:

    • This research identifies a key enzyme involved in nucleoside metabolism in Y. pseudotuberculosis.
    • Understanding this enzyme's function could offer insights into bacterial survival mechanisms and potential therapeutic targets.

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