Role of single-electron reduction potential in inhibition of reverse transcriptase by streptonigrin and sakyomicin A.

نویسندگان

  • Y Inouye
  • K Oogose
  • Y Take
  • T Kubo
  • S Nakamura
چکیده

Streptonigrin was first isolated from Streptomyces flocculus as an antitumor antibiotici;). Later, the antibiotic was recognized to be a potent inhibitor of avian myeloblastosis virus (AMV) reverse transcriptase2). Recently, we reported that streptonigrin inhibited AMV reverse transcriptase mainly by interacting with an enzyme molecule3). According to the results of the kinetic analysis, streptonigrin inhibited reverse transcriptase in a non-competitive manner. As reported previously4~6), the cytotoxicity of streptonigrin results in part from its bypassing effect on the mitochondrial oxidative phosphorylation. In the presence of catalytic amounts of streptonigrin, DT-diaphorase catalyzes the oxidation of NADHsupplied by the mitochondrial redox system. The hydroquinone of streptonigrin formed in conjunction with the oxidation of NADHin turn autoxidizes to the quinone by transferring electrons to molecular oxygen. The electron-acceptor activity of streptonigrin was also observed in the oxidation of NADH by Clostridium kluyveri diaphorase6). Like streptonigrin, sakyomicin A is a quinone antibiotic with an inhibitory activity against reverse transcriptase7» 8) , though the latter is less active than the former. Sakyomicin A played the role of electron acceptor in the oxidation of NADH by both mitochondrial and C. kluyveri diaphorase, as in the case of streptonigrin6»8). Further, we ob-

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Comparative studies of the inhibitory properties of antibiotics on human immunodeficiency virus and avian myeloblastosis virus reverse transcriptases and cellular DNA polymerases.

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Kinetic analysis of inhibition of reverse transcriptase by streptonigrin.

The antitumor antibiotic, streptonigrin (1), was first isolated from Streptomyces flocculus1^. Later, the inhibition of avian myeloblastosis virus (AMV) reverse transcriptase by 1 was reported by Chirigos et al.2\ while no inhibition was observed with methyl streptonigrin (2), suggesting the importance of the carboxyl group for this activity. To confirm this aspect, the biological properties of...

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عنوان ژورنال:
  • The Journal of antibiotics

دوره 40 5  شماره 

صفحات  -

تاریخ انتشار 1987