Recombinant Escherichia coli Constitutive lysine decarboxylase (ldcC) (Active)

Lysine decarboxylase (ldcC) plays a constitutive role in E. coli polyamine biosynthesis by catalyzing the conversion of L-lysine to cadaverine, making it a key target for metabolic pathway studies and antimicrobial research. This full-length recombinant protein (aa 1–713) carries a C-terminal 6xHis tag, positioning the affinity handle away from the catalytic core to minimize interference with substrate access during enzymatic activity assays and kinetic parameter analysis (Km, Vmax, kcat). Functional validation by ELISA confirms binding to E. coli ycbX with an EC50 range of 359–628 μg/ml, demonstrating that the protein adopts a properly folded, interaction-competent conformation suitable for use as a positive control in enzyme-linked assays or for inhibitor screening and IC50 determination. Purity exceeding 85% by SDS-PAGE provides a suitable basis for substrate specificity profiling and preliminary structural studies where high homogeneity supports reproducible measurements.