| Identification | Back Directory | [Name]
ACETYL COENZYME A TRILITHIUM SALT | [CAS]
75520-41-1 | [Synonyms]
C2:0
ACETYL-COA LI3
ACETYL-S-COA LI3
Acet-CoenzymeALi3
ACETYL COENZYME A, LITHIUM
ACETYL-COA TRILITHIUM SALT
Acetyl-S-CoA Li3
ACETYL-COENZYME A, TRILITHIUM
ACETYL COENZYME A LITHIUM SALT
ACETYL COENZYME A TRILITHIUM SALT
Coenzyme A, S-acetate, trilithium salt
Acetyl coenzyme A trilithium salt≥ 92% (UV)
coenzyme A acetyl derivative (C2:0), trilithium salt
ACETYLCOENZYME A TRILITHIUM SALT extrapure for biochemistry | [EINECS(EC#)]
200-790-9 | [Molecular Formula]
C23H35Li3N7O17P3S | [MDL Number]
MFCD00167406 | [MOL File]
75520-41-1.mol | [Molecular Weight]
827.37 |
| Chemical Properties | Back Directory | [Appearance]
White amorphous powder | [storage temp. ]
−20°C
| [solubility ]
Soluble in water (10 mg/ml) | [form ]
solid | [color ]
White | [Stability:]
Stable for 2 years as supplied. Solutions in water may be stored at -20°C for up to 2 weeks. |
| Hazard Information | Back Directory | [Chemical Properties]
White amorphous powder | [Description]
Acetyl-CoA (75520-41-1) is an essential cofactor for cellular metabolism, being an ‘activated acetate’ that shuttles its moieties back and forth during anabolic, catabolic, and metabolic processes involving fundamental molecules: fatty acids, amino acids, glucose, and ATP.1 In the laboratory, it can be used as a substrate in chloramphenicol acetyltransferase (CAT) transcription reporter assays2 or in histone acetyltransferase (HAT) assays in epigenetics research3. | [Uses]
Acetyl Coenzyme?A Lithium Salt is an important molecule in enzymatic acetyl transfer reactions. It is the source of the phosphopantetheine group that is added as a prosthetic group to acyl carrier proteins and formyltetrahydrofolate dehydrogenase. | [in vivo]
Acetyl coenzyme A trilithium blunts pressure overload-induced cardiomyopathy in a mice cardiac pressure overload model by Suppressing maladaptive autophagy[2][3].
Mice deprived of food (but with access to water ad libitum) for 24 h exhibit a significant reduction in total Acetyl coenzyme A levels in several organs, including the heart and muscles, corresponding to a decrease in protein acetylation levels. However, the same experimental conditions have no major effects on Acetyl coenzyme A concentrations in the brain and actually increase hepatic Acetyl coenzyme A and protein acetylation levels[4]. | [References]
Wolfe (2005), The acetate switch; Mol. Biol. Rev. 69 12
Gorman et al. (1982), Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells; Mol. Cell Biol. 2 1044
Kim et al. (2000), A continuous, nonradioactive assay for histone acetyltransferases; Anal. Biochem. 280 308 |
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