Acetyl Coenzyme A (sodium salt)
(Synonyms: 乙酰辅酶A钠盐; Acetyl-CoA trisodium) 目录号 : GC42697
乙酰辅酶A钠盐（Acetyl Coenzyme A (sodium salt)）是酶促乙酰基转移反应中必需的辅因子和酰基载体。Acetyl Coenzyme A 可作为组蛋白乙酰酶（HAT）的乙酰基供体，用于组蛋白和非组蛋白的翻译后乙酰化反应。
Cas No.:102029-73-2
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Acetyl Coenzyme A (sodium salt) is an essential cofactor and acyl carrier in enzymatic acetyl transfer reactions[1]. Acetyl Coenzyme A can serve as an acetyl donor for histone acetylase (HAT) for post-translational acetylation of histones and non-histone proteins[2]. Acetyl Coenzyme A is formed by the oxidative decarboxylation of pyruvate in mitochondria, the oxidation of long-chain fatty acids, or the oxidative degradation of certain amino acids[3]. Acetyl Coenzyme A is the starting compound of the citric acid cycle (Kreb cycle), a key precursor for lipid biosynthesis, and the source of all fatty acid carbons[4]. Acetyl Coenzyme A positively regulates the activity of pyruvate carboxylase[5]. Acetyl Coenzyme A is a precursor of the neurotransmitter acetylcholine[6].
References:
[1] Masiarz F R. Acyl-coenzyme-a: Coenzyme-a Acyltransferase--a Novel Mammalian Enzyme[M]. University of Michigan, 1973.
[2] Takahashi H, McCaffery J M, Irizarry R A, et al. Nucleocytosolic acetyl-coenzyme a synthetase is required for histone acetylation and global transcription[J]. Molecular cell, 2006, 23(2): 207-217.
[3] Abo Alrob O, Lopaschuk G D. Role of CoA and acetyl-CoA in regulating cardiac fatty acid and glucose oxidation[J]. Biochemical Society Transactions, 2014, 42(4): 1043-1051.
[4] Kumar P, Dubey K K. Citric acid cycle regulation: Back bone for secondary metabolite production[M]//New and Future Developments in Microbial Biotechnology and Bioengineering. Elsevier, 2019: 165-181.
[5] Numa S, Tanabe T. Acetyl-coenzyme A carboxylase and its regulation[M]New comprehensive biochemistry. Elsevier, 1984, 7: 1-27.
[6] Szutowicz A, Bielarczyk H, Jankowska-Kulawy A, et al. Acetyl-CoA the key factor for survival or death of cholinergic neurons in course of neurodegenerative diseases[J]. Neurochemical research, 2013, 38: 1523-1542.
乙酰辅酶A钠盐（Acetyl Coenzyme A (sodium salt)）是酶促乙酰基转移反应中必需的辅因子和酰基载体[1]。Acetyl Coenzyme A 可作为组蛋白乙酰酶（HAT）的乙酰基供体，用于组蛋白和非组蛋白的翻译后乙酰化反应[2]。Acetyl Coenzyme A 是由线粒体中丙酮酸的氧化脱羧、长链脂肪酸的氧化或某些氨基酸的氧化降解形成的[3]。Acetyl Coenzyme A 是柠檬酸循环（克雷布循环）的起始化合物，也是脂质生物合成的关键前体，也是所有脂肪酸碳的来源[4]。Acetyl Coenzyme A 正向调节丙酮酸羧化酶的活性[5]。Acetyl Coenzyme A 是神经递质乙酰胆碱的前体[6]。
| Cas No. | 102029-73-2 | SDF | |
| 别名 | 乙酰辅酶A钠盐; Acetyl-CoA trisodium | ||
| Canonical SMILES | O[C@H]1[C@H](N2C=NC3=C2N=CN=C3N)O[C@H](COP(OP(OCC(C)(C)[C@@H](O)C(NCCC(NCCSC(C)=O)=O)=O)(O)=O)(O)=O)[C@H]1OP(O)(O)=O.[Na].[Na].[Na] | ||
| 分子式 | C23H38N7O17P3S•3Na | 分子量 | 878.5 |
| 溶解度 | PBS (pH 7.2): 10 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.1383 mL | 5.6915 mL | 11.383 mL |
| 5 mM | 0.2277 mL | 1.1383 mL | 2.2766 mL |
| 10 mM | 0.1138 mL | 0.5692 mL | 1.1383 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Boosting autofermentation rates and product yields with sodium stress cycling: application to production of renewable fuels by cyanobacteria
Appl Environ Microbiol 2010 Oct;76(19):6455-62.PMID:20693449DOI:10.1128/AEM.00975-10.
Sodium concentration cycling was examined as a new strategy for redistributing carbon storage products and increasing autofermentative product yields following photosynthetic carbon fixation in the cyanobacterium Arthrospira (Spirulina) maxima. The salt-tolerant hypercarbonate strain CS-328 was grown in a medium containing 0.24 to 1.24 M sodium, resulting in increased biosynthesis of soluble carbohydrates to up to 50% of the dry weight at 1.24 M sodium. Hypoionic stress during dark anaerobic metabolism (autofermentation) was induced by resuspending filaments in low-sodium (bi)carbonate buffer (0.21 M), which resulted in accelerated autofermentation rates. For cells grown in 1.24 M NaCl, the fermentative yields of acetate, ethanol, and formate increase substantially to 1.56, 0.75, and 1.54 mmol/(g [dry weight] of cells·day), respectively (36-, 121-, and 6-fold increases in rates relative to cells grown in 0.24 M NaCl). Catabolism of endogenous carbohydrate increased by approximately 2-fold upon hypoionic stress. For cultures grown at all salt concentrations, hydrogen was produced, but its yield did not correlate with increased catabolism of soluble carbohydrates. Instead, ethanol excretion becomes a preferred route for fermentative NADH reoxidation, together with intracellular accumulation of reduced products of Acetyl Coenzyme A (acetyl-CoA) formation when cells are hypoionically stressed. In the absence of hypoionic stress, hydrogen production is a major beneficial pathway for NAD(+) regeneration without wasting carbon intermediates such as ethanol derived from acetyl-CoA. This switch presumably improves the overall cellular economy by retaining carbon within the cell until aerobic conditions return and the acetyl unit can be used for biosynthesis or oxidized via respiration for a much greater energy return.
Characterization of the recombinant diaminobutyric acid acetyltransferase from Methylophaga thalassica and Methylophaga alcalica
FEMS Microbiol Lett 2008 Jun;283(1):91-6.PMID:18410346DOI:10.1111/j.1574-6968.2008.01156.x.
Diaminobutyric acid acetyltransferase (EctA) catalyzes the acetylation of diaminobutyric acid to gamma-N-acetyl-alpha,gamma-diaminobutyrate with Acetyl Coenzyme A. This is the second reaction in the ectoine biosynthetic pathway. The recombinant EctA proteins were purified from two moderately halophilic methylotrophic bacteria: Methylophaga thalassica ATCC 33146T and Methylophaga alcalica ATCC 35842T. EctA found in both methylotrophs is a homodimer with a subunit molecular mass of c. 20 kDa and had similar properties with respect to the optimum temperature for activity (30 degrees C), Km for diaminobutyrate (370 or 375 microM) and the absence of requirements for divalent metal ions. The enzyme from M. thalassica exhibited a lower pH optimum and was inhibited both by sodium carbonates and by high ionic strength but to a lesser extent by copper ions.
Improving culture performance and antibody production in CHO cell culture processes by reducing the Warburg effect
Biotechnol Bioeng 2018 Sep;115(9):2315-2327.PMID:29704441DOI:10.1002/bit.26724.
Lactate is one of the key waste metabolites of mammalian cell culture. High lactate levels are caused by high aerobic glycolysis, also known as the Warburg effect, and are usually associated with adverse culture performance. Therefore, reducing lactate accumulation has been an ongoing challenge in the cell culture development to improve growth, productivity, and process robustness. The pyruvate dehydrogenase complex (PDC) plays a crucial role for the fate of pyruvate, as it converts pyruvate to Acetyl Coenzyme A (acetyl-CoA). The PDC activity can be indirectly increased by inhibiting the PDC inhibitor, pyruvate dehydrogenase kinase, using dichloroacetate (DCA), resulting in less pyruvate being available for lactate formation. Here, Chinese hamster ovary cells were cultivated either with 5 mM DCA or without DCA in various batch and fed-batch bioreactor processes. In all cultures, DCA increased peak viable cell density (VCD), culture length and final antibody titer. The strongest effect was observed in a fed batch with media and glucose feeding in which peak VCD was increased by more than 50%, culture length was extended by more than 3 days, and the final antibody titer increased by more than twofold. In cultures with DCA, lactate production and glucose consumption during exponential growth were on average reduced by approximately 40% and 35%, respectively. Metabolic flux analysis showed reduced glycolytic fluxes, whereas fluxes in the tricarboxylic acid (TCA) cycle were not affected, suggesting that cultures with DCA use glucose more efficiently. In a proteomics analysis, only few proteins were identified as being differentially expressed, indicating that DCA acts on a posttranslational level. Antibody quality in terms of aggregation, charge variant, and glycosylation pattern was unaffected. Subsequent bioreactor experiments with sodium lactate and sodium chloride feeding indicated that lower osmolality, rather than lower lactate concentration itself, improved culture performance in DCA cultures. In conclusion, the addition of DCA to the cell culture improved culture performance and increased antibody titers without any disadvantages for cell-specific productivity or antibody quality.
Evidence for different isotopic enrichments of acetyl-CoA used for cholesterol synthesis in the liver and intestine: a study in the rat by mass fragmentography after intravenous infusion of [13C]acetate
Biochim Biophys Acta 1986 Feb 12;875(2):227-35.PMID:3942765DOI:10.1016/0005-2760(86)90172-4.
Wistar rats were killed 4 h after an intravenous infusion of [1,2-13C]- and [1-14C]acetic acid sodium salt (39 mg, 12.5 microCi/ml, constant rate: 1.2 ml/h). At this time, labeled free cholesterol movements between the organs are still weak and cholesterol labeling in each tissue mainly originates from the in situ incorporation of the exogenous substrate. In male rats, the specific radioactivity of free cholesterol was found to be higher in the intestine (mucosa and wall) than in the liver and plasma. In female and in cholestyramine-fed male rats, cholesterol 14C labeling was close to that of male rats in the intestine, and was markedly higher in the liver. The same variations of 13C excess, calculated by mass fragmentography, indicated that there was no isotopic effect between 13C and 14C precursors. The advantage of this method consisted in obtaining the proportions of labeled molecules according to their molecular weight (M + 1-M + 11) for each sample. Then the distribution of 13C atoms in newly synthesized cholesterol was assessed in each sterogenesis site. In the intestine, about 3/4 of the 13C atoms were found in molecules of weight of at least M + 4 (after incorporation of at least two labeled acetate units). This proportion was only 1/3 in hepatic and plasma free cholesterol. These distinct 13C-labeling patterns clearly indicate that local variations occurred in the isotopic enrichment of acetyl-CoA used for cholesterol formation. Whatever the experimental conditions of this study, cholesterol was synthesized from an acetyl-CoA more 13C enriched in the intestine than in the liver. Such variations probably result from the different dilutions of exogenous acetyl-CoA by the endogenous pool in the liver and intestine. Consequently, the 14C or 13C incorporations measured in the liver and intestinal sterols do not account for absolute rates of cholesterol production by these organs. This study also indicated that after a few hours of infusion, free cholesterol labeling in the plasma originated mainly from cholesterol newly formed in the liver, even when acetate incorporation into cholesterol was higher in the intestine than in the liver.
Multiple forms of choline-O-acetyltransferase in mouse and rat brain: solubilization and characterization
J Neurochem 1983 Oct;41(4):1030-9.PMID:6619842DOI:10.1111/j.1471-4159.1983.tb09047.x.
Three forms of Acetyl Coenzyme A: choline-O-acetyltransferase (EC 2.3.1.6, ChAT) have been isolated from mouse and rat forebrain synaptosomes with a 100 mM sodium phosphate (NaP) buffer of pH 7.4, a high-salt solution (500 mM NaCl), and a 2% Triton DN-65 solution, respectively. The Triton-solubilized form of ChAT differed from the other two forms in its capacity to acetylate homocholine, its pH profile, and its sensitivity to denaturation. NaCl-solubilized ChAT could be distinguished from the other two forms with respect to pH profile, sensitivity to inhibition by 4-(1-naphthylvinyl) pyridine (in the presence of Triton), and apparent Km value for choline acetylation. The caudate and putamen of rat brain contained the highest amount of ChAT activity, based on tissue wet weight, and the cerebellum contained the least of the brain regions examined; only the cerebellum had more membrane-bound than soluble ChAT. Septal lesion reduced ChAT activity in the NaP- and Triton-solubilized fractions prepared from hippocampus by 68% and 64%, respectively, whereas it reduced the activity of the NaCl-solubilized fraction by only 21%. These results suggest that three different forms of ChAT may exist in both mouse and rat brain.