Functional Characterization and Unraveling the Structural Determinants of Novel Steroid Hydroxylase CYP154C7 from Streptomyces sp. PAMC26508
October 2024
in “
Heliyon
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TLDR CYP154C7 enzyme can effectively modify steroids and is promising for commercial use.
The study explores the cytochrome P450 enzyme CYP154C7 from Streptomyces sp. PAMC26508, which effectively hydroxylates steroids, particularly at the 16α-position, with a high affinity for androstenedione. Optimal activity occurs at 30°C and pH 7.4. Key residues, lysine (K236) and tyrosine (Y197), are crucial for substrate selectivity and catalytic efficiency. The enzyme's potential as a biocatalyst was demonstrated in E. coli, suggesting its promise for developing modified steroids. Homology modeling and docking studies provide insights into substrate binding and catalytic efficiency, underscoring CYP154C7's potential in steroid bioconversion and biotechnological applications.