@article{mbs:/content/journal/micro/10.1099/13500872-142-12-3347, author = "Usuda, Yoshihiro and Tujimoto, Nobuharu and Abe, Chizu and Asakura, Yoko and Kimura, Eiichiro and Kawahara, Yoshio and Kurahashi, Osamu and Matsui, Hiroshi", title = "Molecular cloning of the Corynebacterium glutamicum (‘Brevibacterium lactofermentum’ AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase", journal= "Microbiology", year = "1996", volume = "142", number = "12", pages = "3347-3354", doi = "https://doi.org/10.1099/13500872-142-12-3347", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-142-12-3347", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "odhAgene", keywords = "Keywords: Corynebacterium glutamicum,", keywords = "2-oxoglutarate dehydrogenase", keywords = "‘Brevibacterium lactofermentum’,", abstract = "The Corynebacterium glutamicum (‘Brevibacterium lactofermentum’ AJ12036) odhA gene, encoding 2-oxoglutarate dehydrogenase (E1o subunit of the 2-oxoglutarate dehydrogenase complex), has been isolated and identified as an homologous counterpart of the Escherichia coli sucA and Bacillus subtilis odhA genes. The nucleotide sequence of a 4394 bp chromosomal fragment containing the C. glutamicum odhA gene was determined. The odhA gene comprised 3771 bp (1257 codons, including the initiation codon) and a molecular mass of 138656 Da was predicted for the OdhA polypeptide. Northern blot analysis revealed a 3·9 kb transcript. The size of the transcript, together with the presence of a rho-independent terminator-like structure, suggests that C. glutamicum odhA is monocistronic. Cells harbouring plasmids carrying C. glutamicum odhA showed a threefold increase in specific 2-oxoglutarate dehydrogenase complex activity and expression of a protein with an apparent molecular mass of 136 kDa, in good agreement with the predicted size of the OdhA polypeptide. The C-terminal region of the C. glutamicum OdhA protein shows strong sequence similarity to E1os from other organisms. C. glutamicum OdhA has an N-terminal extension not found in previously reported E1os. The amino acid sequence of this extension shows similarity to that of the C-terminal region of dihydrolipoamide S-succinyltransferase (E2o) subunits of 2-oxoglutarate dehydrogenase complexes and dihydrolipoamide S-acetyltransferase (E2p) subunits of pyruvate dehydrogenase complexes. It suggests that the C. glutamicum odhA gene might encode a novel bifunctional protein with E1o and E2o activities.", }