The present invention provides a bacterium of the genus Corynebacterium, in particular of the species Corynebacterium glutamicum, having the ability to excrete an L-amino acid selected from proteinogenic L-amino acids and L-omithine and new measures for the fermentative production of proteinogenic L-amino acids and L-ornithine by such bacteria.

The present invention provides a bacterium of the genus Corynebacterium, in particular of the species Corynebacterium glutamicum, having the ability to excrete an L-amino acid selected from proteinogenic L-amino acids and L-omithine and new measures for the fermentative production of proteinogenic L-amino acids and L-ornithine by such bacteria.

The invention relates to reagents and methods that allow the expression of an active NifB protein in yeast and plants under aerobic conditions. The active NifB protein allows the in vitro synthesis of the FeMo cofactor (FeMo-co) which leads to the subsequent apo-NifDK activation and generation of active nitrogenase.

The invention relates to reagents and methods that allow the expression of an active NifB protein in yeast and plants under aerobic conditions. The active NifB protein allows the in vitro synthesis of the FeMo cofactor (FeMo-co) which leads to the subsequent apo-NifDK activation and generation of active nitrogenase.

The invention relates to a recombinant, L-amino acid-secreting microorganism of the Enterobacteriaceae family, comprising an DNA fragment having promoter activity that is functionally linked to a polynucleotide coding for a membrane protein, characterized in that the DNA fragment having promoter activity comprises the SEQ ID NO: 8.

The invention relates to a recombinant, L-amino acid-secreting microorganism of the Enterobacteriaceae family, comprising an DNA fragment having promoter activity that is functionally linked to a polynucleotide coding for a membrane protein, characterized in that the DNA fragment having promoter activity comprises the SEQ ID NO: 8.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.