BACKGROUND ATP Citrate Lyase (ACL) is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues and has a central role in de novo lipid synthesis. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis.1 In nervous tissue, ATP Citrate-Lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene.2
Three phosphorylation sites have been identified on ACL, namely threonine 446, serine 450, and serine 454. It is phosphorylated by GSK-3 on Thr446 and Ser450, and by PKA and Akt on Ser454. Phosphorylation on Ser454 abolishes the homotropic allosteric regulation by citrate and enhances the catalytic activity of the enzyme.3
1. Ramakrishna, S. et al: Biochem. 29:7617-24, 1990
2. Hughes, K. et al: Biochem. J. 15:309-14, 1992
3. Berwick, D.C. et al: J. Biol. Chem. 277:33895-900, 2002
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