The maeA enzyme belongs to the malic enzyme family, which plays critical roles in microbial metabolism, including maintaining redox balance, energy production, and carbon flux regulation . In Pectobacterium carotovorum, a plant pathogen, malic enzymes may contribute to pathogenicity by modulating metabolic pathways during host invasion . The recombinant form is a truncated or partial version, likely engineered to study specific biochemical or structural features.
Current literature lacks detailed biochemical data on maeA, including:
Kinetic Parameters: Optimal pH, temperature, and substrate specificity.
Structural Insights: Domain organization and cofactor-binding motifs.
Functional Studies: Role in Pectobacterium’s metabolic networks or pathogenicity.
For comparison, recombinant endo-polygalacturonase (endo-PGase) from Pectobacterium has been characterized in Bacillus subtilis, showing optimal activity at pH 5.0 and 40°C . Similar approaches could be applied to maeA to elucidate its catalytic properties.
Metabolic Engineering: Engineering maeA to modulate redox balance in microbial systems for biofuel production.
Pathogen Research: Investigating its role in Pectobacterium’s metabolic adaptation during infection .
Biocatalysis: Exploiting its enzymatic activity for malate-to-pyruvate conversion in industrial processes.