Fig. 3: Terminal truncation of RnHO-1 and RnCPR improves soluble expression without compromising enzymatic activity.
From: Systemic engineering and global regulation enabling high-level bilirubin biosynthesis
a Hydrophobicity analysis of RnCPR and RnHO-1 reveals hydrophobic membrane-associating regions at the N-terminus of RnCPR (residues 1–54) and C-terminus of RnHO-1 (residues 268–289). These regions were systematically truncated to enhance soluble expression. b SDS-PAGE analysis of soluble expression levels in E. coli BL21 (DE3) shows increased expression with progressive truncation, with RnCPRΔ54 and RnHO-1Δ22 exhibiting the highest solubility, the experiment was independently repeated three times, with consistent results. c, Michaelis–Menten kinetic parameters (Km and kcat/Km) of wild-type and truncated RnHO-1 and RnCPR variants. All truncation mutants retain comparable catalytic efficiency. RnBVR is included as a control; kinetic parameters were not determined (N.D.) due to strong substrate inhibition. N.A., not applicable. Source data are provided as a Source Data file.
