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  • Title: Inhibition of DNA polymerases by tripeptide derivative protease inhibitors.
    Author: Taguchi T, Matsukage A, Ito H, Saito Y, Kawashima S.
    Journal: Biochem Biophys Res Commun; 1992 Jun 30; 185(3):1133-40. PubMed ID: 1627135.
    Abstract:
    Benzyloxycarbonyl(Z)-Leu-Leu-Leu-al and dansyl(Dns)-Leu-Leu-Leu-CH2Cl, well known as protease inhibitors, effectively inhibit the activities of DNA polymerases alpha, beta and gamma from rat liver and pol I from Escherichia coli, but the ability of these inhibitors to inhibit terminal deoxynucleotidyl transferase (TdT) is weak. The mode of inhibition by these tripeptide analogues is non-competitive with dNTP. The Ki values for Z-Leu-Leu-Leu-al and Dns-Leu-Leu-Leu-CH2Cl are 6.25 x 10(-5) M and 6.56 x 10(-5) M, respectively.
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