EC Number   |
General Information |
Reference |
|---|
   2.3.1.7 | malfunction |
enzyme deficiency increases tissue acetyl-CoA levels and susceptibility to diet-induced lysine acetylation of broad-ranging mitochondrial proteins, coincident with diminished whole body glucose control |
735906 |
| 2.3.1.7 | malfunction |
silencing the CrAT gene disrupts cellular carnitine homeostasis, reduces the expression of mitochondrial superoxide dismutase 2 and results in an increase in oxidative stress within the mitochondrion |
736268 |
| 2.3.1.7 | physiological function |
carnitine acetyltransferase Yat1 is cytosolic and contributes to acetyl-CoA transport from the cytosol during growth on ethanol or acetate, but its activity is not required for growth on oleate |
719875 |
| 2.3.1.7 | physiological function |
Crat deletion in Aguoti-related peptide neurons reduces food intake and feeding behavior and increases glycerol supply to the liver during fasting, as a gluconeogenic substrate. Crat deletion increases peripheral fatty acid substrate utilization and attenuates the switch to glucose utilization after refeeding. Crat regulates protein acetylation and metabolic processing |
756398 |
| 2.3.1.7 | physiological function |
in the murine cardiomyocyte cytosol, reverse CrAT activity (producing acetyl-CoA) is higher compared with the liver. The heart displays a lower reverse CrAT Km for CoA compared with the liver. Cytosolic reverse CrAT accounts for 4.6% of total activity in heart tissue and 12.7% in H9C2 cells, while highly purified heart cytosolic fractions show significant CrAT protein levels. Acetyl-CoA carboxylase ACC2-knockout mouse hearts show decreased CrAT protein levels and activity, associated with increased palmitate oxidation and acetyl-CoA/CoA ratio compared with controls. Feeding mice a high-fat diet for 10 weeks increases cardiac CrAT protein levels and activity, associated with a reduced acetyl-CoA/CoA ratio and glucose oxidation |
756008 |
| 2.3.1.7 | physiological function |
mitochondrial carnitine acetyltransferase Cat2 is required for the intramitochondrial conversion of acetylcarnitine to acetyl-CoA, which is essential for a functional tricarboxylic acid cycle during growth on oleate, acetate, ethanol, and citrate. Peroxisomal Cat2 is essential neither for export of acetyl units during growth on oleate nor for the import of acetyl units during growth on acetate or ethanol. Oxidation of fatty acids still takes place in the absence of peroxisomal Cat2, but biomass formation is absent, and the strain displays a growth delay on acetate and ethanol that can be partially rescued by the addition of carnitine |
719875 |
| 2.3.1.7 | physiological function |
protein is essential for growth on fatty acids as well as acetate. Mislocalization of the enzyme to the cytoplasm does not result in loss of growth on acetate but prevents growth on fatty acids. The mitochondrial enzyme is essential for the transfer of acetyl units to mitochondria, peroxisomal localization is required only for transfer from peroxisomes to mitochondria. Peroxisomal enzyme is not required for the import of acetyl-CoA into peroxisomes for conversion to malate by malate synthase, and export of acetyl-CoA from peroxisomes to the cytoplasm is independent of FacC when malate synthase is mislocalized to the cytoplasm |
719381 |
| 2.3.1.7 | physiological function |
the enzyme inhibits mitochondrial acetyl-CoA overload by regulating the efflux of acetyl-CoA, thus maintaining PDH activity in skeletal muscle |
736560 |
| 2.3.1.7 | physiological function |
the enzyme mitigates metabolic inertia and muscle fatigue during exercise |
735903 |
| 2.3.1.7 | physiological function |
the enzyme plays a role in modulating the muscle acetylproteome |
735906 |
