Application | Comment | Organism |
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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 | Pseudomonas putida |
Protein Variants | Comment | Organism |
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additional information | 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 | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
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Pseudomonas putida | - |
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- |
Pseudomonas putida KT 2240 | - |
- |
- |