CHARACTERIZATION OF TRYPANOSOMA-BRUCEI-BRUCEI S-ADENOSYL-L-METHIONINE DECARBOXYLASE AND ITS INHIBITION BY BERENIL, PENTAMIDINE AND METHYLGLYOXAL BIS(GUANYLHYDRAZONE)
CHARACTERIZATION OF TRYPANOSOMA-BRUCEI-BRUCEI S-ADENOSYL-L-METHIONINE DECARBOXYLASE AND ITS INHIBITION BY BERENIL, PENTAMIDINE AND METHYLGLYOXAL BIS(GUANYLHYDRAZONE)
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DOI：
10.1042/bj2370685
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发表时间：
1986-08-01
影响因子：
4.1
通讯作者：
MCCANN, PP
中科院分区：
文献类型：
--
作者：
BITONTI, AJ;DUMONT, JA;MCCANN, PP
Trypanosoma brucei brucei S-adenosyl-L-methionine (AdoMet) decarboxylase was found to be relatively insensitive to activation by putrescine as compared with the mammalian enzyme, being stimulated by only 50% over a 10,000-fold range of putrescine concentrations. The enzyme was not stimulated by up to 10 mM-Mg2+. The Km for AdoMet was 30 .mu.M, similar to that of other eukaryotic AdoMet decarboxylases. T. b. brucei AdoMet decarboxylase activity was apparently irreversibly inhibited in vitro by Berenil and reversibly by pentamidine and methylglyoxal bis(guanylhydrazone). Berenil also inhibited trypanosomal AdoMet decarboxylase by 70% within 4 h after administration to infected rats and markedly increased the concentration of putrescine in trypanosomes that were exposed to the drug in vivo. Spermidine and spermine blocked the curative effect of Berenil on model mouse T. b. brucei infections. This effect of the polyamines was probably not due to reversal of Berenil''s inhibitory effects on the AdoMet decarboxylase.
