Cloned (Comment) | Organism |
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expression in Corynebacterium glutamicum | Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
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General Information | Comment | Organism |
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physiological function | heterologous expression in Corynebacterium glutamicum leads to a recombinant protein that is insensitive to fructose 1-phosphate and fructose 2,6-bisphosphate, whereas the homologous fructose-1,6-bisphosphatase is inhibited by fructose 1-phosphate and fructose 2,6-bisphosphate. The relative enzyme activity of heterologous fructose-1,6-bisphosphatase is 90.8% and 89.1% during supplement with 3 mM fructose 1-phosphate and fructose 2,6-bisphosphate, respectively. Phosphoenolpyruvate is an activator of heterologous fructose-1,6-bisphosphatase, whereas the homologous fructose-1,6-bisphosphatase is very sensitive to phosphoenolpyruvate. Overexpression of the heterologous fructose 1,6-bisphosphatase in wild-type Corynebacterium glutamicum has no effect on L-lysine production, but fructose-1,6-bisphosphatase activities are increased 9- to 13fold. Overexpression increases L-lysine production in Corynebacterim glutamicum lysC(T311I) by 57.3% on fructose, 48.7% on sucrose, and 43% on glucose. The dry cell weight and maximal specific growth rate are increased by overexpression of heterologous fructose 1,6-bisphosphatase | Escherichia coli |