Loading...
The shikimate pathway is a vital metabolic route in bacteria, fungi, and plants, leading to the biosynthesis of aromatic amino acids (tryptophan, tyrosine, phenylalanine). Two key enzymes in this pathway—recombinant dehydratase-synthase and recombinant Escherichia coli shikimate dehydrogenase (AroE)—are gaining importance in synthetic biology, bioprocess optimization, and antibiotic development.
Genprice
Scientific Publications
Shikimate dehydrogenase (EC 1.1.1.25), encoded by the aroE gene in Escherichia coli, catalyzes the reversible reduction of 3-dehydroshikimate to shikimate, using NADPH as a cofactor. This is the fifth step in the shikimate pathway, critical for microbial viability and absent in mammals—making AroE a target for antimicrobial drug development.
The term dehydratase-synthase refers to enzymes that perform dehydration and condensation reactions, often in biosynthetic pathways such as polyketide synthesis, fatty acid metabolism, or amino acid biosynthesis. In the shikimate pathway, such enzymatic activities assist in ring closures and intermediate transformations.
Recombinant AroE and dehydratase enzymes are used to reconstruct the shikimate pathway in heterologous hosts like E. coli, yeast, and Corynebacterium glutamicum to produce:
Because the shikimate pathway is absent in humans, AroE is studied as a selective dru g target for:
Recombinant AroE is typically cloned into a plasmid vector (e.g., pET, pBAD), expressed in E. coli BL21 (DE3), and purified using :
Protein purity is confirmed using SDS-PAGE and Western blotting, and activity is measured via NADPH consumption assays at 340 nm.
