ⓘ Lanosterol 14 alpha-demethylase

                                     

ⓘ Lanosterol 14 alpha-demethylase

Lanosterol 14α-demethylase is a cytochrome P450 enzyme that is involved in the conversion of lanosterol to 4.4-dimethylcholesta-8.14.24-trien-3β-ol. The cytochrome P450 isoenzymes are a conserved group of proteins that serve as key players in the metabolism of organic substances and the biosynthesis of important steroids, lipids, and vitamins in eukaryotes. As a member of this family, lanosterol 14α-demethylase is responsible for an essential step in the biosynthesis of sterols. In particular, this protein catalyzes the removal of the C-14α-methyl group from lanosterol. This demethylation step is regarded as the initial checkpoint in the transformation of lanosterol to other sterols that are widely used within the cell.

Although lanosterol 14α-demethylase is present in a wide variety of organisms, this enzyme is seen mainly in the context of fungi, where it plays an important role in mediating membrane permeability. In fungi, CYP51 catalyzes lanosterol demethylation to create an important precursor that eventually turns into ergosterol. Then this steroid makes his way across the cell, where it alters the permeability and rigidity of plasma membranes how much cholesterol in animals. Because ergosterol is a major component of fungal membrane, many antifungal drugs have been developed to suppress 14α-demethylase activities and to prevent the production of such a composite key.