Literature DB >> 1510731

Inhibition of enzymes of polyamine back-conversion by pentamidine and berenil.

P R Libby1, C W Porter.   

Abstract

Pentamidine and berenil, clinical antiparasitic amidines, have been found to be potent competitive inhibitors of human spermidine/spermine acetyltransferase (SSAT). Ki values were found to be 2.4 and 2 microM, respectively, with spermidine as substrate. A second enzyme of polyamine back-conversion, murine polyamine oxidase (PAO), was found to be competitively inhibited by pentamidine, with a Ki of 7.6 microM when N-acetylspermine was the substrate. Berenil, on the other hand, was an extremely weak inhibitor (Ki = 120 microM). The implication of the effect of inhibition of polyamine back-conversion on the growth of mammalian parasites is discussed.

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Year:  1992        PMID: 1510731     DOI: 10.1016/0006-2952(92)90424-h

Source DB:  PubMed          Journal:  Biochem Pharmacol        ISSN: 0006-2952            Impact factor:   5.858


  9 in total

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4.  Reduction in polyamine catabolism leads to spermine-mediated airway epithelial injury and induces asthma features.

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6.  Association Between Plasma Diacetylspermine and Tumor Spermine Synthase With Outcome in Triple-Negative Breast Cancer.

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7.  Effects of pentamidine isethionate on Saccharomyces cerevisiae.

Authors:  G Ludewig; J M Williams; Y Li; C Staben
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  9 in total

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