Esherichia coli B strain was genetically engineered to produce L-alanine as the primary fermentation product from sugars by replacing the native D-lactate dehydrogenase of E. coli SZ194 with alanine dehydrogenase from Geobacillus stearothermophilus. The resulting strain, XZ111, accumulated alanine as the primary product during glucose fermentation. The methylgloxyal synthase gene (mgsA) was deleted to eliminate low levels of lactate and improve growth, and the catabolic alanine racemace gene (dadX) was deleted to minimize conversion of L-alanine to D-alanine. In the resulting strain, NADH oxidation during alanine biosynthesis is obligately linked to ATP production and cell growth. This linkage provided a basis for metabolic evolution where selection for improvements in growth co-selected for increased glycolytic flux and alanine production. The resulting strain, XZ132, produced 1279 mM alanine from 120 g l^-1 glucose within 48 h during batch fermentation in mineral salts medium. The alanine yield was 95% on a weight basis (g g^-1 glucose) with a chiral purity greater than 99.5% L-alanine.