Physicochemical Properties of Malate Dehydrogenase from the Bacterium Rhodopseudomonas palustris Strain f8pt

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A. T. Eprintsev^1*, M. I. Falaleeva¹, M. A. Klimova¹, and E. I. Kompantseva²

¹Voronezh State University, Universitetskaya pl. 1, 394006 Voronezh, Russia; fax: (4732) 208-755; E-mail: bc366@bio.vsu.ru

²Vinogradsky Institute of Microbiology, Russian Academy of Sciences, pr. 60-letiya Oktyabrya 7, 117811 Moscow, Russia; fax: (495) 135-6530; E-mail: elenamaxi@mail.ru

^* To whom correspondence should be addressed.

Received December 14, 2005; Revision received February 7, 2006

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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.

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KEY WORDS: malate dehydrogenase, purification, dimer, tetramer, catalytic properties

DOI: 10.1134/S000629796060149

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