sterol 14-demethylase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.13.70 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a sterol 14-demethylase (EC 1.14.13.70) is an enzyme of the cytochrome P450 (CYP) superfamily. It is any member of the CYP51 family. It catalyzes a chemical reaction such as:
The 4 substrates here are obtusifoliol, O2, NADPH, and H+, whereas its 4 products are 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol, formate, NADP+, and H2O.
Although the lanosterol 14α-demethylase is present in a wide variety of organisms, the enzyme is studied primarily in the context of fungi, where it plays an essential role in mediating membrane permeability.[1] In fungi, CYP51 catalyzes the demethylation of lanosterol to create an important precursor that is eventually converted into ergosterol.[2] 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.[3] 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.[3]
Lepesheva_2007
was invoked but never defined (see the help page).