Squalene monooxygenase
Squalene monooxygenase (also known as squalene epoxidase) is an enzyme that plays a crucial role in the sterol biosynthesis pathway. This enzyme is responsible for the conversion of squalene into 2,3-oxidosqualene (squalene epoxide). Squalene monooxygenase is a key enzyme in the cholesterol biosynthesis pathway and is considered a potential target for cholesterol-lowering drugs.
Function[edit | edit source]
Squalene monooxygenase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway. It catalyzes the conversion of squalene to 2,3-oxidosqualene and requires NADPH and oxygen as substrates.
Structure[edit | edit source]
The enzyme is a membrane-bound protein located in the endoplasmic reticulum. It contains a flavoprotein domain that binds FAD and a NAD(P)H-binding domain. The enzyme is thought to have a single transmembrane domain near the N-terminus.
Clinical significance[edit | edit source]
Due to its role in cholesterol biosynthesis, squalene monooxygenase is a target for cholesterol-lowering drugs such as statins. Inhibition of this enzyme can lead to a decrease in cholesterol synthesis, which can be beneficial in the treatment of diseases such as hypercholesterolemia and atherosclerosis.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD