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Literature summary for 3.1.3.11 extracted from

  • Xu, J.Z.; Zhang, J.L.; Guo, Y.F.; Jia, Q.D.; Zhang, W.G.
    Heterologous expression of Escherichia coli fructose-1,6-bisphosphatase in Corynebacterium glutamicum and evaluating the effect on cell growth and L-lysine production (2014), Prep. Biochem. Biotechnol., 44, 493-509.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Corynebacterium glutamicum Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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General Information

General Information Comment Organism
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