Stearoyl-coa desaturase
Stearoyl-CoA desaturase (SCD) is an enzyme that plays a crucial role in fatty acid metabolism. It is involved in the biosynthesis of monounsaturated fatty acids (MUFAs), which are essential components of cell membranes and also serve as substrates for the synthesis of lipid signaling molecules.
Function[edit | edit source]
Stearoyl-CoA desaturase catalyzes the rate-limiting step in the synthesis of MUFAs. Specifically, it converts saturated fatty acids (SFAs) into MUFAs by introducing a double bond into the fatty acid chain. The primary substrates for this reaction are stearoyl-CoA and palmitoyl-CoA, which are converted into oleoyl-CoA and palmitoleoyl-CoA, respectively.
Structure[edit | edit source]
The enzyme is a membrane protein that is located in the endoplasmic reticulum. It consists of four transmembrane domains and contains a cytochrome b5 domain that is required for its enzymatic activity. The active site of the enzyme is located in the lumen of the endoplasmic reticulum.
Clinical significance[edit | edit source]
Alterations in the activity of Stearoyl-CoA desaturase have been implicated in a variety of diseases, including obesity, type 2 diabetes, cardiovascular disease, and cancer. In particular, increased SCD activity has been associated with increased lipogenesis and the development of insulin resistance.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD