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РЖ ВИНИТИ 34 (BI48) 96.10-04Т2.370

Competition between inhibitors of the trypanosome alternative oxidase (TAO) and reduced coenzyme Q[9] [Text] / Georgios Pollakis [et al.] // Biochem. Pharmacol. - 1995. - Vol. 50, N 8. - P1207-1210 . - ISSN 0006-2952
Перевод заглавия: Конкуренция между ингибиторами альтернативной оксидазы трипаносом (ТАО) и восстановленной формой кофермента Q[9]
Аннотация: The trypanosome alternative oxidase (TAO) is an attractive target for chemotherapy for the diseases cuased by African trypanosomes because there is no equivalent enzyme in mammalian hosts. Many inhibitors of this enzyme have been described, but there have been no data on the mechanism of inhibition. In the present study, reduced 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone (decyl-CoQ-H[2]) was used as a substitute for the natural substrate CoQ[9]-H[2] to allow direct measurements of the TAO in crude mitochondrial preparations from Trypanosoma brucei brucei. A K[m] value of 3.8 'мю'M was obtained for this substrate. The following five compounds that have alkyl side chains from 1 to 4 carbons and belong to three classes of inhibitors showed a competitive inhibition pattern with respect to decyl-CoQ-H[2]: p-methoxybenzhydroxamic acid, p-ethoxybenzhydroxamic acid, p-n-butyloxybenzhydroxamic acid, methyl 3,4-dihydroxybenzoate and N-n-butyl-3,4-dihydroxybenzamide. The following four compounds belonging to the same chemical classes but having alkyl side chains from 10 to 12 carbons showed uncompetitive inhibition patterns: p-n-dodecyloxybenzhydroxamic acid, n-decyl 3,4-dihydroxybenzoate, n-dodecyl 3,4-dihydroxybenzoate, and N-n-decyl-3,4-dihydroxybenzamide. Clearly, the first group of inhibitors compete with CoQ-H[2] for the active site of the TAO. It was proposed that the uncompetitive patterns produced by the second group of inhibitors are due to the greater lipophilicity of these compounds and the resulting change in the interaction of the inhibitors and the membrane containing the TAO, thus affecting the local concentration of the inhibitors at the active site. США, Dep. of Medical and Molecular Parasitology, New York Univ. Medical Center, New York, NY 10016. Библ. 17

ГРНТИ	34.45.21

ВИНИТИ 341.45.21.95.41.99
Рубрики: ПРОТИВОПРОТОЗОЙНЫЕ СРЕДСТВА
ИНГИБИТОРЫ
АЛЬТЕРНАТИВНАЯ ОКСИДАЗА ТРИПАНОСОМ
МЕХАНИЗМ ДЕЙСТВИЯ
КОФЕРМЕНТ Q[9]
ВОССТАНОВЛЕННАЯ ФОРМА

Доп.точки доступа:
Pollakis, Georgios; Grady, Robert W.; Dieck, Harold A.; Clarkson, Allen B.

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