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J. Biol. Chem., Vol. 262, Issue 5, 2187-2189, 02, 1987
YC Cheng, GE Dutschman, KF Bastow, MG Sarngadharan and RY Ting
Using affinity purified human immunodeficiency virus (HIV) reverse
transcriptase the reaction assay conditions were determined. The optimum
incorporation of dTMP into the (rA)n(dT)10 template with HIV reverse
transcriptase required 6 mM MgCl2 and 80 mM KCl. The template specificity
of HIV reverse transcriptase is quite different from those of the human
gamma-polymerase-associated reverse transcriptase or avian virus reverse
transcriptase. The preferential inhibition of HIV reverse transcriptase as
compared to human gamma-reverse transcriptase was observed with several
nucleoside analog triphosphates. The Ki values for thymidine triphosphate
analogs with HIV reverse transcriptase ranged from 5 to 13 nM with
decreasing effectiveness for 3'-fluoro greater than 3'-amino greater than
2',3'-dideoxy greater than 3'-azido groups. This study provides information
on the structure activity relationships of the triphosphate analogs
inhibitory effects on HIV reverse transcriptase versus human
gamma-polymerase-associated reverse transcriptase, and the possible
mechanisms of action of 3' azido thymidine and the
2',3'-dideoxynucleosides, and also identifies other nucleoside analogs for
possible development as inhibitors of HIV.
Human immunodeficiency virus reverse transcriptase. General properties and its interactions with nucleoside triphosphate analogs
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