EC Number   |
Application |
Reference |
|---|
    2.6.1.48 | synthesis |
expression of the Pseudomonas putida davAB genes encoding delta-aminovaleramidase and lysine 2-monooxygenase, respectively, in Escherichia coli. When the davAB genes are introduced into recombinant E. coli strain XQ56 allowing enhanced L-lysine synthesis, 0.27 and 0.5g/l of 5-aminovalerate are produced directly from glucose by batch- and fed-batch cultures, respectively. Further conversion of 5-aminovalerate into glutarate can be achieved by expression of the Pseudomonas putida gabTD genes encoding 5-aminovalerate aminotransferase and glutarate semialdehyde dehydrogenase. In a medium containing 20g/l glucose, 10g/l L-lysine and 10g/l alpha-ketoglutarate, this strain produces 1.7g/l of glutarate |
-, 728239 |
| 2.6.1.48 | synthesis |
production of 5-aminovalerate and glutarate in Escherichia coli. Endogenous over-production of the precursor, lysine, is first achieved through metabolic deregulation of its biosynthesis pathway by introducing feedback resistant mutants of aspartate kinase III and dihydrodipicolinate synthase. Further disruption of native lysine decarboxylase activity limits cadaverine by-product formation. Co-expression of lysine monooxygenase and 5-aminovaleramide amidohydrolase then results in the production of 0.86 g/l 5-aminovalerate in 48 h. The additional co-expression of glutaric semialdehyde dehydrogenase and 5-aminovalerate aminotransferase leads to the production of 0.82 g/l glutarate under the same conditions. Yields on glucose are 71 and 68 mmol/mol for 5-aminovalerate and glutarate, respectively |
-, 721885 |
| 2.6.1.48 | synthesis |
production of 5-aminovalerate and glutarate in recombinant Escherichia coli. When the davAB genes encoding delta-aminovaleramidase and lysine 2-monooxygenase, respectively, are introduced into a recombinant Escherichia coli strain allowing enhanced L-lysine synthesis, 0.27 and 0.5 g/l of 5-aminovalerate are produced directly from glucose by batch and fed-batch cultures, respectively. Further conversion of 5-aminovalerate into glutarate can be demonstrated by expression of the Pseudomonas putida gabTD genes encoding 5-aminovalerate aminotransferase and glutarate semialdehyde dehydrogenase. A recombinant Eschrerichia coli strain expressing the davAB and gabTD genes cultured in a medium containing 20 g/l glucose,10 g/l L-lysine and 10 g/l alpha-ketoglutarate, produces 1.7 g/l of glutarate |
723096 |
