Phospho-Acetyl-CoA Carboxylase (Ser79) is a phosphorylated form of Acetyl-CoA Carboxylase (ACC), a key enzyme in lipid metabolism that catalyzes the conversion of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. When phosphorylated at Ser79, ACC is inhibited, preventing the production of malonyl-CoA and thus suppressing fatty acid synthesis. This phosphorylation is primarily regulated by AMP-activated protein kinase (AMPK), which is activated under low energy conditions, such as fasting, to promote fatty acid oxidation and conserve energy. ACC exists in two isoforms, ACC1 and ACC2, with ACC1 mainly involved in fatty acid synthesis and ACC2 regulating fatty acid oxidation by inhibiting carnitine palmitoyltransferase I (CPT-I) in mitochondria. Phospho-ACC (Ser79) antibodies are widely used to detect the phosphorylated state of ACC in various tissues and species, including human, mouse, and rat.
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