Reference: Ravera S, et al. (2010) Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Mol Biol (Mosk) 44(3):472-6

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Abstract


Glucose-6-phosphate 1 dehydrogenase (G6PD) is a ubiquitous enzyme catalyzing the oxidation of D-glucose 6-phosphate to D-glucono-lactone 6-phosphate, in the first step of the pentose phosphate pathway. Based on the currently available structural information on Leuconostoc mesenteroides G6PD, it is believed that the enzyme only works as a homodimer. Here we show that both after non-denaturing and after denaturing electrophoretic separation (SDS-PAGE) and blotting L. mesenteroides G6PD retains its complete catalytic activity. In the two latter cases the molecular weight of the band corresponded to that of a G6PD monomer. Conversely, when the same technique was applied to G6PD from Saccharomyces cerevisiae, another fermentative organism, the monomer activity was not detectable after SDS-PAGE and blotting. The results are discussed in terms of molecular evolution of the oligomeric state in the various G6PD sources.

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Journal Article
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Ravera S, Calzia D, Morelli A, Panfoli I
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