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The pyruvate dehydrogenase (PDH) complex of the gram-negative bacteriumZymomonas mobilis was purified to homogeneity. From 250 g of cells, we isolated 1 mg of PDH complex with a specific activity of 12.6 U/mg of protein. Analysis of subunit composition revealed a PDH (E1) consisting of the two subunits E1α (38 kDa) and E1β (56 kDa), a dihydrolipoamide acetyltransferase (E2) of 48 kDa, and a lipoamide dehydrogenase (E3) of 50 kDa. The E2 core of the complex is arranged to form a pentagonal dodecahedron, as shown by electron microscopic images, resembling the quaternary structures of PDH complexes from gram-positive bacteria and eukaryotes. The PDH complex-encoding genes were identified by hybridization experiments and sequence analysis in two separate gene regions in the genome ofZ. mobilis . The genespdhA α (1,065 bp) andpdhA β (1,389 bp), encoding the E1α and E1β subunits of the E1 component, were located downstream of the gene encoding enolase. ThepdhB (1,323 bp) andlpd (1,401 bp) genes, encoding the E2 and E3 components, were identified in an unrelated gene region together with a 450-bp open reading frame (ORF) of unknown function in the orderpdhB -ORF2-lpd . Highest similarities of the gene products of thepdhA α,pdhA β, andpdhB genes were found with the corresponding enzymes ofSaccharomyces cerevisiae and other eukaryotes. Like the dihydrolipoamide acetyltransferases ofS. cerevisiae and numerous other organisms, the product of thepdhB gene contains a single lipoyl domain. The E1β subunit PDH was found to contain an amino-terminal lipoyl domain, a property which is unique among PDHs.

journal of bacteriology

Purification of the Pyruvate Dehydrogenase Multienzyme Complex of <i>Zymomonas mobilis</i> and Identification and Sequence Analysis of the Corresponding Genes

Purification of the Pyruvate Dehydrogenase Multienzyme Complex of Zymomonas mobilis and Identification and Sequence Analysis of the Corresponding Genes