Physicochemical properties of malate dehydrogenase from the bacterium Rhodopseudomonas palustris strain f8pt.
Electrophoretically homogenous isoforms of malate dehydrogenase with different quaternary structure were prepared from Rhodopseudomonas palustris strain f8pt cultured photolithoheterotrophically on malate and acetate. By selective inhibition of the tricarboxylic acid cycle or glyoxylate cycle, it was shown that the dimeric isoform of the enzyme is responsible for Krebs cycle functioning and the tetrameric isoform is involved in functioning of the glyoxylate cycle.
Eprintsev
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Voronezh State University, Voronezh, 394006, Russia. bc366@bio.vsu.ru
Falaleeva
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MI
Klimova
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MA
Kompantseva
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EI
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D008291:Malate Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification; D020836:Protein Structure, Quaternary; D012241:Rhodopseudomonas / Q000201:enzymology* / Q000254:growth & development
D001426:Bacterial Proteins; D007527:Isoenzymes; D008291:Malate Dehydrogenase