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Inhibition of DNA Polymerases by Tripeptide Derivative Protease Inhibitors

Inhibition of DNA Polymerases by Tripeptide Derivative Protease Inhibitors

T Taguchi, A Matsukage, H Ito, Y Saito, S Kawashima

Biochem Biophys Res Commun. 1992 Jun 30;185(3):1133-40.

PMID: 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP133407826-D	Z-Leu-Leu-Leu-al		133407-82-6	Price

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