Acyl CoA dehydrogenase
Acyl CoA dehydrogenase is a family of enzymes that play a crucial role in the metabolism of fatty acids by catalyzing the dehydrogenation of acyl-CoA derivatives. These enzymes are involved in the beta-oxidation process, where they facilitate the breakdown of fatty acids to produce energy.
Structure[edit | edit source]
Acyl CoA dehydrogenases are flavoproteins, meaning they contain a flavin adenine dinucleotide (FAD) molecule as a prosthetic group. The FAD molecule is essential for the enzyme's catalytic activity. The enzymes are typically composed of four identical subunits, each containing a FAD molecule.
Function[edit | edit source]
The primary function of acyl CoA dehydrogenase is to catalyze the first step in the beta-oxidation of fatty acids. This involves the dehydrogenation of acyl-CoA derivatives, which results in the formation of a double bond between the alpha and beta carbon atoms. The electrons removed during this process are transferred to the FAD molecule, reducing it to FADH2. The FADH2 molecule then transfers these electrons to the electron transport chain, contributing to the production of ATP.
Clinical significance[edit | edit source]
Deficiencies in acyl CoA dehydrogenase can lead to a variety of metabolic disorders. For example, medium-chain acyl-CoA dehydrogenase deficiency (MCADD) is a condition that prevents the body from converting certain fats to energy, particularly during periods of fasting. Similarly, very long-chain acyl-CoA dehydrogenase deficiency (VLCADD) affects the body's ability to break down certain fats. Both conditions can lead to a buildup of fatty acids in the body, which can be harmful.
See also[edit | edit source]
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