ATP citrate synthase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: acetyl-CoA + ADP + H+ + oxaloacetate + phosphate = ATP + citrate + CoA. [RHEA:21160]

ATP citrate lyase (ACL) is an enzyme that catalyzes the reversible cleavage of citrate into oxaloacetate and acetyl-CoA, using ATP and CoA as cofactors. This reaction is a key step in the glyoxylate cycle, a metabolic pathway that allows organisms to utilize acetate as a carbon source. In mammals, ACL is primarily found in the cytoplasm of adipocytes, where it plays a role in fatty acid synthesis. It also participates in the regulation of lipogenesis and gluconeogenesis. ACL uses ATP to break the bond between the carboxyl group on the citrate molecule and the carbon atom adjacent to it, forming oxaloacetate and acetyl-CoA. The mechanism involves the transfer of the CoA group from CoA to the acetyl group of citrate, followed by the cleavage of the C-C bond. ACL requires magnesium ions for its activity. Mutations in the ACL gene can lead to a variety of metabolic disorders, including hyperammonemia, hypoglycemia, and hyperlipidemia.'
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Proteins (1)

Compounds (2)