Acetate—CoA Ligase (ADP-forming)
Acetate—CoA Ligase (ADP-forming) is an enzyme that catalyzes the chemical reaction of converting acetate, ATP, and CoA into AMP, diphosphate, and acetyl-CoA. This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is acetate:CoA ligase (ADP-forming).
Function[edit | edit source]
Acetate—CoA Ligase (ADP-forming) plays a crucial role in the metabolism of fatty acids. It is involved in the activation of acetate, a two-carbon molecule, for incorporation into fatty acids and other acetyl derivatives. This enzyme is also involved in the citric acid cycle, a key metabolic pathway that connects carbohydrate, fat, and protein metabolism.
Structure[edit | edit source]
The enzyme is composed of two domains: the larger domain is responsible for the binding of CoA and the smaller domain is responsible for the binding of ATP. The active site is located in a cleft between the two domains.
Clinical significance[edit | edit source]
Alterations in the activity of Acetate—CoA Ligase (ADP-forming) have been associated with various diseases, including diabetes and obesity. Increased activity of this enzyme can lead to an overproduction of acetyl-CoA, which can contribute to the development of these conditions.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD