Lipoamide dehydrogenase from corynebacterium glutamicum: molecular and physiological analysis of the lpd gene and characterization of the enzyme

Article Abstract:

Research describes the molecular and physiological characterizattion of the lipoamide dehydrogenase and its gene, lpd, in Corynebacterium glutamicum. Results reveal that lpd gene is monocistronic and translates into a 1.45 kilobase mRNA, encoding a product of approximately 51 kilodalton with 26 and 58% identity to other lipoamide dehydrogenases.

Germany, France, Statistical Data Included, Analysis, Enzymes, Microbial metabolism, Gene expression, Gram-positive bacteria, Enzyme structure-activity relationships

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Pyruvate carboxylase as an anaplerotic enzyme in Corynebacterium glutamicum

Article Abstract:

The significance of Pyruvate carboxylase (PCx) for the growth of Corynebacterium glutamicum was studied. Evidence that C. glutamicum possessed PCx and phosphoenol-pyruvate carboxylase (PEPCx) was presented. PCx functioned as an anaplerotic enzyme during growth on glucose and lactate in the absence and even in the presence of PEPCx, respectively. PCx was found to have no anaplerotic significance for growth on acetate as carbon source.

Bacteria, Chemical reactions

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Pyruvate carboxylase from Corynebacterium glutamicum: characterization, expression and inactivation of the pyc gene

Article Abstract:

The gene for pyruvate carboxylase (PCx) from Corynebacterium glutamicum is identified using a 200 base pair probe and cloned through polymerase chain reaction. The gene is designated as pyc and its product is predicted to be a polypeptide containing 1,140 amino acid residues. Transcriptional studies revealed that pyc is monocistronic. PCx enable C. glutamicum to utilize lactate as a carbon source.

Genetic aspects, Microbial enzymes

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