Lanosterol 14-alpha demethylase

Cytochrome P450, Family 51, Subfamily A, Polypeptide 1
Identifiers
Symbol	CYP51A1
Alt. symbols	CYP51, P45014DM
Entrez	1595
HUGO	2649
OMIM	601637
RefSeq	NM_000786
UniProt	Q16850
Other data
EC number	1.14.13.70
Locus	Chr. 7 q21.2-21.3

Lanosterol 14α-demethylase (or CYP51A1) is a enzyme that is involved in the conversion of lanosterol to 4,4-dimethylcholesta-8(9),14,24-trien-3β-ol. The 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 (Lepesheva et al.). This demethylation step is regarded as the initial checkpoint in the transformation of lanosterol to other sterols that are widely used within the cell (Lepesheva et al.).

Although lanosterol 14α-demethylase is present in a wide variety of organisms, this enzyme is studied primarily in the context of fungi, where it plays an essential role in mediating membrane permeability. In fungi, CYP51 catalyzes the demethylation of lanosterol to create an important precursor that is eventually converted into ergosterol (Lepesheva et al.). This steroid then makes its way throughout the cell, where it alters the permeability and rigidity of plasma membranes much as cholesterol does in animals. Because ergosterol constitutes a fundamental component of fungal membranes, many antifungal medications have been developed to inhibit 14α-demethylase activity and prevent the production of this key compound (Becher et al.).

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