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Effect of C-4'-modification of thiamine pyrophosphate on its coenzyme activity in the oxidative decarboxylation of pyruvic acid reactionстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 20 апреля 2016 г.
- Авторы: Severin S.E., Khailova L.S., Bernkhardt R.
- Журнал: Ukrainskii Biokhimicheskii Zhurnal
- Том: 48
- Номер: 4
- Год издания: 1976
- Издательство: National'na Akademiya Nauk Ukrainy
- Местоположение издательства: Ukraine
- Первая страница: 503
- Последняя страница: 509
- Аннотация: Interaction was studied between pyruvate dehydrogenase (EC 1.2.4.1) and C-4'-substituted analogs of thiaminpyrophosphate, 4'-N (CH3)-TPP, 4'-N(CH3)2-TPP and OH-TPP. None of these analogs was found to replace TPP during the reduction of NAD and 2.6-dichlorophenol-indophenol as well as pyruvate decarboxylation. The decarboxylase activity of the pyruvate dehydrogenase component isolated from the pyruvate dehydrogenase complex was determined according to the 14CO2 yield and production of 2-C-oxoethyl-TPP using 1-14C-pyruvate and 2-14C-pyruvate, as substrates, respectively. All the analogs were found to competitively inhibit pyruvate dehydrogenase, Ki values for 4'-N(CH3)-TPP, 4'-N(CH3)2-TPP and 4'-OH-TPP being 4.1 X 10(-5) M, 8.5 X 10(-5) M and 2.9 X 10(-6) M, respectively; Km values for TPP was equal to 1-2 X 10(-7) M. It is assumed that the analogs of the holoenzymic complex formed by the pyruvate dehydrogenase component of the pyruvate dehydrogenase complex with mono-, dimethyl-TPP and oxo-TPP do not bind the substrate.
- Добавил в систему: Хайлова Людмила Самуиловна