ArticleProtein science : a publication of the Protein Society2019
Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Evidence for ecological adaptation of reductive citric acid and reverse oxidative citric acid cycles based on a survey of genomes from autotrophicFEMS microbes · 2026Review
- SIRT2-mediated deacetylation of ACLY promotes the progression of oesophageal squamous cell carcinoma.Journal of cellular and molecular medicine · 2024Article
- Allosteric role of the citrate synthase homology domain of ATP citrate lyase.Nature communications · 2023Article
- The structure of succinyl-CoA synthetase bound to the succinyl-phosphate intermediate clarifies the catalytic mechanism of ATP-citrate lyase.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Acetyl-CoA is produced by the citrate synthase homology module of ATP-citrate lyase.Nature structural & molecular biology · 2021Article
- Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
ATP-citrate lyase (ACLY) catalyzes production of acetyl-CoA and oxaloacetate from CoA and citrate using ATP. In humans, this cytoplasmic enzyme connects energy metabolism from carbohydrates to the production of lipids. In certain bacteria, ACLY is used to fix carbon in the reductive tricarboxylic acid cycle. The carboxy(C)-terminal portion of ACLY shows sequence similarity to citrate synthase of the tricarboxylic acid cycle. To investigate the roles of residues of ACLY equivalent to active site residues of citrate synthase, these residues in ACLY from Chlorobium limicola were mutated, and the proteins were investigated using kinetics assays and biophysical techniques. To obtain the crystal structure of the C-terminal portion of ACLY, full-length C. limicola ACLY was cleaved, first non-specifically with chymotrypsin and subsequently with Tobacco Etch Virus protease. Crystals of the C-terminal portion diffracted to high resolution, providing structures that show the positions of active site residues and how ACLY tetramerizes.
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