Dissecting the Roles of the N- and C-Flanking Residues of Acetyllysine Substrates for SIRT1 Activity

Authors

  • Roman Meledin,

    1. Department of Life Sciences and the National Institute for Biotechnology in the Negev (NIBN), Ben-Gurion University of the Negev, Be'er Sheva 84105 (Israel)
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  • Prof. Ashraf Brik,

    Corresponding author
    1. Department of Chemistry3, Ben-Gurion University of the Negev, Be'er Sheva 84105 (Israel)
    • Department of Chemistry3, Ben-Gurion University of the Negev, Be'er Sheva 84105 (Israel)
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  • Prof. Amir Aharoni

    Corresponding author
    1. Department of Life Sciences and the National Institute for Biotechnology in the Negev (NIBN), Ben-Gurion University of the Negev, Be'er Sheva 84105 (Israel)
    • Department of Life Sciences and the National Institute for Biotechnology in the Negev (NIBN), Ben-Gurion University of the Negev, Be'er Sheva 84105 (Israel)
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Abstract

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SIRT1 specificity: The multispecific SIRT1 enzyme catalyzes the deacetylation of acetyllysine residues within protein targets. However, little is known regarding the molecular basis for SIRT1 substrate recognition. Kinetic analysis of SIRT1 with a panel of peptide substrates shows the high importance of the region N-flanking the target acetyllysine and its high conservation through evolution.

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