ATP citrate synthase

ATP citrate synthase is an enzyme that plays a crucial role in the cellular respiration process, specifically in the citric acid cycle. It is responsible for catalyzing the conversion of citrate and CoA into oxaloacetate and acetyl-CoA, a key step in the cycle.

Function

ATP citrate synthase is primarily located in the mitochondria, where it facilitates the production of acetyl-CoA from citrate and CoA. This reaction is a crucial part of the citric acid cycle, also known as the Krebs cycle or the tricarboxylic acid (TCA) cycle. The cycle is a series of chemical reactions used by all aerobic organisms to release stored energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins into adenosine triphosphate (ATP) and carbon dioxide.

ATP citrate synthase catalyzes the conversion of citrate and CoA into oxaloacetate and acetyl-CoA.

Structure

ATP citrate synthase is a homodimer, meaning it is composed of two identical subunits. Each subunit is composed of a large domain and a small domain. The large domain is involved in the binding of citrate, while the small domain is involved in the binding of CoA.

Clinical significance

Alterations in the activity of ATP citrate synthase have been implicated in several diseases, including cancer, diabetes, and neurodegenerative diseases. For example, increased activity of ATP citrate synthase has been observed in some types of cancer, suggesting that this enzyme may be a potential target for cancer therapy.

See also

• Citric acid cycle
• Enzyme
• Mitochondria

References

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