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Inhibition of DNA polymerases by tripeptide derivative protease inhibitors
T Taguchi1, A Matsukage, H Ito
1Department of Molecular Biology, Tokyo Metropolitan Institute of Gerontology, Japan.
Biochemical and Biophysical Research Communications
|June 30, 1992
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.