Literature DB >> 8495733

Inactivation of alpha-ketoglutarate dehydrogenase during oxidative decarboxylation of alpha-ketoadipic acid.

V I Bunik1, O G Pavlova.   

Abstract

alpha-Ketoglutarate dehydrogenase was inactivated irreversibly and completely during oxidation of alpha-ketoadipic acid. The inactivation was revealed both in the model system with ferricyanide and in the overall reaction catalyzed by the alpha-ketoglutarate dehydrogenase complex. Neither substrate depletion nor product accumulation induced the inactivation. The results obtained were compared with recent data on the enzyme inactivation during oxidation of alpha-ketoglutaric acid. The differences in the inactivation kinetics observed with the two substrates of the enzyme were analyzed. They seem not to reflect the different mechanisms of the inactivation, but, rather, depend on the changes in the rates of the individual stages of the process.

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Year:  1993        PMID： 8495733     DOI： 10.1016/0014-5793(93)81472-c

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  5 in total

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2.  Regulation of oxidative degradation of L-lysine in rat liver mitochondria.

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Review 4.  Enzyme-catalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases.

Authors:  Victoria I Bunik; John V Schloss; John T Pinto; Gary E Gibson; Arthur J L Cooper
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5.  Synthetic analogues of 2-oxo acids discriminate metabolic contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases in mammalian cells and tissues.

Authors:  Artem V Artiukhov; Aneta Grabarska; Ewelina Gumbarewicz; Vasily A Aleshin; Thilo Kähne; Toshihiro Obata; Alexey V Kazantsev; Nikolay V Lukashev; Andrzej Stepulak; Alisdair R Fernie; Victoria I Bunik
Journal:  Sci Rep       Date:  2020-02-05       Impact factor: 4.379
  5 in total

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