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Target intelligence / Profile preview
Squalene Epoxidase (Fungal) (SE)
- Target
- SE
- Molecular classification
- Enzyme, Flavoprotein monooxygenase
01
Overview
Squalene epoxidase (SE), also known as squalene monooxygenase, is a key flavin adenine dinucleotide (FAD)-dependent enzyme involved in the ergosterol biosynthetic pathway in fungi. It catalyzes the conversion of squalene to 2,3-oxidosqualene, a crucial step for producing ergosterol, which maintains membrane integrity and function. SE is a validated target for antifungal drugs, particularly allylamines like terbinafine, which inhibit the enzyme and disrupt ergosterol synthesis. Inhibition leads to accumulation of squalene and depletion of ergosterol, disrupting membrane function and causing fungicidal effects.
- Other names
- Squalene monooxygenaseFungal Squalene Epoxidase
02
Mechanism of action
Noncompetitive inhibition via conformational change, preventing substrate (squalene) binding.
03
Biological functions
Ergosterol biosynthesisSterol biosynthesisMembrane integrity maintenance
04
Disease associations
Infection
05
Safety considerations
Potential for drug resistance through mutations in the active site.Off-target effects, though less likely than with cytochrome P450 inhibitors.
06
Interacting drugs
Terbinafine
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