Glucose-6-phosphate isomerase (pgi) is a key enzyme in glycolysis, catalyzing the reversible isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P) . In Escherichia coli, this enzyme is critical for maintaining metabolic flux balance between the glycolytic pathway and the pentose phosphate pathway (PPP) . The recombinant form of E. coli pgi, particularly from the O17:K52:H18 strain, is studied for its biochemical properties, structural insights, and applications in metabolic engineering.
Pgi facilitates the interconversion of G6P and F6P, enabling carbon flux through glycolysis and PPP .
Loss of pgi reroutes metabolism to the PPP, increasing NADPH production and activating compensatory pathways like the glyoxylate shunt .
Δpgi mutants exhibit slow growth, reliance on PPP, and acetate/formate overflow metabolism .
Adaptive evolution in Δpgi strains involves mutations in rpoS, udhA, and pntAB to restore redox balance .
Recombinant pgi is produced via heterologous expression in systems like E. coli or yeast. Key product specifications include:
Recombinant pgi retains catalytic activity similar to native E. coli pgi .
Heterologous PGIs (e.g., from archaea) can substitute for E. coli pgi, albeit with reduced growth rates .
Pgi modulation is explored to optimize biofuel production (e.g., ethanol) and reduce acetate overflow .
Deletion of pgi enhances PPP-dependent pathways, useful for synthesizing NADPH-rich metabolites .
Pgi inhibitors disrupt sugar metabolism in pathogens like Aspergillus flavus, affecting virulence .
Structural studies of pgi guide rational drug design for targeting metabolic vulnerabilities .
| Feature | E. coli pgi | Archaeal pgi (e.g., Pyrococcus furiosus) |
|---|---|---|
| Thermal Stability | Moderate | High |
| Catalytic Efficiency | Optimized for glucose | Adapted to non-phosphorylated substrates |
| Host Expression | E. coli (common) | E. coli or heterologous systems |
KEGG: eum:ECUMN_4558