EC Number   |
General Information |
Reference |
|---|
    2.3.3.1 | malfunction |
citrate synthase activity reduction leads to a strong L-lysine accumulation |
719138 |
| 2.3.3.1 | metabolism |
citrate synthase is a key enzyme of the citric acid cycle that provides energy for cellular function. Additionally, the enzyme plays a critical role in providing citrate derived acetyl-CoA for lipogenesis and cholesterologenesis |
720857 |
| 2.3.3.1 | metabolism |
Clostridium thermocellum carries both Re- and Si-citrate synthases, i.e. EC 2.3.3.3 and EC 2.3.3.1, respectively, to initiate the tricarboxic acid cycle |
756796 |
| 2.3.3.1 | metabolism |
the enzyme is required for both tricarboxylic acid and glyoxylic acid cycle activity |
720082 |
| 2.3.3.1 | more |
sequences and structures of citrate synthases from the psychrophile antarctic bacterium DS2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility |
744711 |
| 2.3.3.1 | more |
sequences and structures of citrate synthases from the psychrophile Arthobacter Ds2-3R, from chicken, and from the hyperthermophile Pyrococcus furiosus are compared. The three enzymes share similar packing, burial of nonpolar surface area, and main-chain hydrogen bonding. However, both psychrophilic and hyperthermophilic citrate synthases contain more charged residues, salt bridges, and salt-bridge networks than the mesophile. The electrostatic free energy contributions toward protein stability by individual charged residues show greater variabilities in the psychrophilic citrate synthase than in the hyperthermophilic enzyme. The charged residues in the active-site regions of the psychrophile are more destabilizing than those in the active-site regions of the hyperthermophile.In the hyperthermophilic enzyme, salt bridges and their networks largely cluster in the active-site regions and at the dimer interface. In contrast, in the psychrophile, they are more dispersed throughout the structure. On average, salt bridges and their networks provide greater electrostatic stabilization to the thermophilic citrate synthase at 100°C than to the psychrophilic enzyme at 0°C. Electrostatics appears to play an important role in both heat and cold adaptation of citrate synthase. However, remarkably, the role may be different in the two types of enzyme: In the hyperthermophile, it may contribute to the integrity of both the protein dimer and the active site by possibly countering conformational disorder at high temperatures. On the other hand, in the psychrophile at low temperatures, electrostatics may contribute to enhance protein solvation and to ensure active-site flexibility |
744711 |
| 2.3.3.1 | physiological function |
during high-fat diet feeding, glucose tolerance of mice decreases progressively and to a greater extent in females with low citrate synthase activity compared to wild-type females, with males showing a similar trend. Body weight and fat gain does not differ between low CS activity and wild-type mice. After an 18 h incubation in 0.8 mM palmitate, C2C12 muscle cells with about 50% shRNA-mediated reduction in CS activity show lower viability and increased levels of cleaved caspase-3 compared to the scramble shRNA treated C2C12 cells |
757468 |
| 2.3.3.1 | physiological function |
the citrate synthase gene is a direct retinoic acid receptor-related orphan receptor alpha target and one mechanism by which retinoic acid receptor-related orphan receptor alpha regulates lipid metabolism is via regulation of citrate synthase expression |
720857 |
