EC Number   |
|---|
   4.3.1.1 | - |
| 4.3.1.1 | although Corynebacterium glutamicum posses the aspartate ammonia-lyase gene (aspA), aspartate aminotransferase (AAT) is necessary to cell growth and L-lysine production, because the activity of Corynebacterium glutamicum aspartate ammonia-lyase (AAL) is too low to maintain the cell growth. Escherichia coli aspartate ammonia-lyase helps to restore the cell growth of aspB-deleted strain and also leads to the accumulation of L-lysine, L-glutamate, pyruvate and 2-oxoglutarate |
| 4.3.1.1 | An aspartase mutant 81-176 unable to utilize any amino acid except serine (defective in microaerobic growth on multiple amino acids) and an aspA sdaA double-mutant (also lacking serine dehydratase) is cloned. The aspA gene is cloned into the pET101 expression vector and overexpressed in Escherichia coli BL21 |
| 4.3.1.1 | AspB is expressed in Escherichia coli |
| 4.3.1.1 | cloned and overexpressed in Escherichia coli TOP10 |
| 4.3.1.1 | cloning in the pLATE31 plasmid composition and highly efficient expression under the control of the T7 phage promoter in Escherichia coli BLR (DE3) cell. The use of the expression system allows an increase in aspartase activity in cells by 100times as compared to the initial strain. The maximal specific activity of cells reached 0.700 mM/mg/min |
| 4.3.1.1 | expression in Escherichia coli |
| 4.3.1.1 | expression in Escherichia coli BL21 |
| 4.3.1.1 | expression of His-tagged wild-type enzyme and His-tagged mutant enzyme K327N in Escherichia coli |
| 4.3.1.1 | functional and inactive aspA are cloned and expressed in AspA-deficient Escherichia coli |
