Artigo Acesso aberto Revisado por pares

Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli α-ketoglutarate dehydrogenase complex

1979; Elsevier BV; Volume: 192; Issue: 1 Linguagem: Inglês

10.1016/0003-9861(79)90099-7

ISSN

1096-0384

Autores

Subhash Gupta, Eugene E. Dekker,

Tópico(s)

Amino Acid Enzymes and Metabolism

Resumo

Enzyme preparations from pig heart and Escherichia coli have been found to catalyze a NAD+- and CoASH-dependent oxidation of 2-keto-4-hydroxyglutarate. Several independent lines of evidence indicate that 2-keto-4-hydroxyglutarate is a substrate for the well-known α-ketoglutarate dehydrogenase complex of the citric acid cycle. The evidence includes (a) a constant ratio of specific activity values for the two substrates throughout purification, (b) identical elution profiles from a Ca3(PO4)2 gel-cellulose column, (c) the same sucrose density sedimentation patterns, (d) similar responses in controlled heat inactivation studies, and (e) identical pH-activity curves.

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