cis-Epoxysuccinic acid
目录号 : GC67837cis-Epoxysuccinic acid 是 succinate receptor (SUCNR1/GPR91) 的激动剂。cis-Epoxysuccinic acid 抑制 cAMP 的水平，其 EC50 值为 2.7 µM。cis-Epoxysuccinic acid 可用于心血管系统的研究。
Cas No.:16533-72-5
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
cis-Epoxysuccinic acid is a succinate receptor (SUCNR1/GPR91) agonist. cis-Epoxysuccinic acid inhibits cAMP levels with an EC50 value of 2.7 µM. cis-Epoxysuccinic acid can be used for the research of cardiovascular system[1].
cis-Epoxysuccinic acid (1-100 μM; 10 min) affects cAMP levels of HEK293 cells[1].
cis-Epoxysuccinic acid (0.1 μM-100 mM; 1 h) agonists SUCNR1 pathways without affects succinate dehydrogenase[1].
Cell Viability Assay[1]
| Cell Line: | HEK293 cells |
| Concentration: | 1, 10 and 100 μM |
| Incubation Time: | 10 min |
| Result: | Inhibited cAMP levels with an EC50 value of 2.7 µM. |
Cell Viability Assay[1]
| Cell Line: | HEK293 cells |
| Concentration: | 0.1 μM-100 mM |
| Incubation Time: | 1 hour |
| Result: | Induced the Gq pathway, recruited arrestin 3 and elicited [Ca2+]i mobilization with EC50 values of 42, 74 and 191 µM, respectively. |
cis-Epoxysuccinic acid (1 mg/kg; i.v. once) has an effect on the blood pressure of rats[1].
| Animal Model: | Male Wistar rats[1] |
| Dosage: | 1 mg/kg |
| Administration: | Intravenous injection; 1 mg/kg once |
| Result: | Showed in vivo activity and increased blood pressure after injection. |
[1]. Geubelle P, et al. Identification and pharmacological characterization of succinate receptor agonists. Br J Pharmacol. 2017 May;174(9):796-808.
| Cas No. | 16533-72-5 | SDF | Download SDF |
| 分子式 | C4H4O5 | 分子量 | 132.07 |
| 溶解度 | DMSO : ≥ 250 mg/mL (1892.94 mM) | 储存条件 | 4°C, protect from light |
| 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 | 7.5717 mL | 37.8587 mL | 75.7174 mL |
| 5 mM | 1.5143 mL | 7.5717 mL | 15.1435 mL |
| 10 mM | 0.7572 mL | 3.7859 mL | 7.5717 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。
Optimization of culture conditions for production of cis-Epoxysuccinic acid hydrolase using response surface methodology
Bioresour Technol 2008 Sep;99(13):5391-6.PMID:18083551DOI:10.1016/j.biortech.2007.11.017.
Response surface methodology, which allows for rapid identification of important factors and optimization of them to enhance enzyme production, was employed here to optimize culture conditions for the production of cis-Epoxysuccinic acid hydrolase from Bordetella sp. strain 1-3. In the first step, a Plackett-Burman design was used to evaluate the effects of nine variables (yeast extract, cis-Epoxysuccinic acid, KH(2)PO(4), K(2)HPO(4).3H(2)O, MgSO(4).7H(2)O, trace minerals solution, culture volume, initial pH and incubation time) on the enzyme production. Yeast extract, cis-Epoxysuccinic acid and KH(2)PO(4) had significant influences on cis-Epoxysuccinic acid hydrolase production and their concentrations were further optimized using central composite design and response surface analysis. A combination of adjusting the concentration of yeast extract to 7.8 g/l, cis-Epoxysuccinic acid to 9.8 g/l, and KH(2)PO(4) to 1.12 g/l would favor maximum cis-Epoxysuccinic acid hydrolase production. An enhancement of cis-Epoxysuccinic acid hydrolase production from 5.6 U/ml to 9.27 U/ml was gained after optimization.
Purification and characterization of a cis-Epoxysuccinic acid hydrolase from Nocardia tartaricans CAS-52, and expression in Escherichia coli
Appl Microbiol Biotechnol 2013 Mar;97(6):2433-41.PMID:22552902DOI:10.1007/s00253-012-4102-4.
A highly enantioselective cis-Epoxysuccinic acid hydrolase from Nocardia tartaricans was purified to electrophoretic homogeneity. The enzyme was purified 184-fold with a yield of 18.8 %. The purified cis-Epoxysuccinic acid hydrolase had a monomeric molecular weight of 28 kDa, and its optimum conditions were 37 °C and pH 7-9. With sodium cis-epoxysuccinate as the substrate, Michaelis-Menten enzyme kinetics analysis gave a Km value of 35.71 mM and a Vmax of 2.65 mM min(-1). The enzyme was activated by Ni(2+) and Al(3+), while strongly inhibited by Fe(3+), Fe(2+), Cu(2+), and Ag(+). The cis-Epoxysuccinic acid hydrolase gene was cloned, and its open reading frame sequence predicted a protein composed of 253 amino acids. A pET11a expression plasmid carrying the gene under the control of the T7 promoter was introduced into Escherichia coli, and the cis-Epoxysuccinic acid hydrolase gene was successfully expressed in the recombinant strains.
Purification and characterization of a cis-Epoxysuccinic acid hydrolase from Bordetella sp. strain 1-3
Protein Expr Purif 2010 Jan;69(1):16-20.PMID:19800407DOI:10.1016/j.pep.2009.09.018.
Purification of a cis-Epoxysuccinic acid hydrolase was achieved by ammonium sulfate precipitation, ionic exchange chromatography, hydrophobic interaction chromatography followed by size-exclusion chromatography. The enzyme was purified 177-fold with a yield of 14.4%. The apparent molecular mass of the enzyme was determined to be 33kDa under denaturing conditions. The optimum pH for enzyme activity was 7.0, and the enzyme exhibited maximum activity at about 45 degrees C in 50mM sodium phosphate buffer (pH 7.5). EDTA and o-phenanthrolin inhibited the enzyme activity remarkably, suggesting that the enzyme needs some metal cation to maintain its activity. Results of inductively coupled plasma mass spectrometry analysis indicated that the cis-Epoxysuccinic acid hydrolase needs Zn(2+) as a cofactor. Eight amino acids sequenced from the N-terminal region of the cis-Epoxysuccinic acid hydrolase showed the same sequence as the N-terminal region of the beta subunit of the cis-Epoxysuccinic acid hydrolase obtained from Alcaligenes sp.
Efficiency and stability enhancement of cis-Epoxysuccinic acid hydrolase by fusion with a carbohydrate binding module and immobilization onto cellulose
Appl Biochem Biotechnol 2012 Oct;168(3):708-17.PMID:22843080DOI:10.1007/s12010-012-9811-8.
cis-Epoxysuccinic acid hydrolase (CESH) is an enzyme that catalyzes cis-Epoxysuccinic acid to produce enantiomeric L(+)-tartaric acid. The production of tartaric acid by using CESH would be valuable in the chemical industry because of its high yield and selectivity, but the low stability of CESH hampers its application. To improve the stability of CESH, we fused five different carbohydrate-binding modules (CBMs) to CESH and immobilized the chimeric enzymes on cellulose. The effects of the fusion and immobilization on the activity, kinetics, and stability of CESH were compared. Activity measurements demonstrated that the fusion with CBMs and the immobilization on cellulose increased the pH and temperature adaptability of CESH. The chimeric enzymes showed significantly different enzyme kinetics parameters, among which the immobilized CBM30-CESH exhibited twofold catalytic efficiency compared with the native CESH. The half-life measurements indicated that the stability of the enzyme in its free form was slightly increased by the fusion with CBMs, whereas the immobilization on cellulose significantly increased the stability of the enzyme. The immobilized CBM30-CESH showed the longest half-life, which is more than five times the free native CESH half-life at 30 °C. Therefore, most CBMs can improve enzymatic properties, and CBM30 is the best fusion partner for CESH to improve both its enzymatic efficiency and its stability.
High yield recombinant expression, characterization and homology modeling of two types of cis-Epoxysuccinic acid hydrolases
Protein J 2012 Jun;31(5):432-8.PMID:22592448DOI:10.1007/s10930-012-9418-5.
The cis-epoxysuccinate hydrolases (CESHs), members of epoxide hydrolase, catalyze cis-Epoxysuccinic acid hydrolysis to form D: (-)-tartaric acid or L: (+)-tartaric acid which are important chemicals with broad scientific and industrial applications. Two types of CESHs (CESH[D: ] and CESH[L: ], producing D: (-)- and L: (+)-tartaric acids, respectively) have been reported with low yield and complicated purification procedure in previous studies. In this paper, the two CESHs were overexpressed in Escherichia coli using codon-optimized genes. High protein yields by one-step purifications were obtained for both recombinant enzymes. The optimal pH and temperature were measured for both recombinant CESHs, and the properties of recombinant enzymes were similar to native enzymes. Kinetics parameters measured by Lineweaver-Burk plot indicates both enzymes exhibited similar affinity to cis-Epoxysuccinic acid, but CESH[L: ] showed much higher catalytic efficiency than CESH[D: ], suggesting that the two CESHs have different catalytic mechanisms. The structures of both CESHs constructed by homology modeling indicated that CESH[L: ] and CESH[D: ] have different structural folds and potential active site residues. CESH[L: ] adopted a typical α/β-hydrolase fold with a cap domain and a core domain, whereas CESH[D: ] possessed a unique TIM barrel fold composed of 8 α-helices and 8 β-strands, and 2 extra short α-helices exist on the top and bottom of the barrel, respectively. A divalent metal ion, preferred to be zinc, was found in CESH[D: ], and the ion was proved to be crucial to the enzymatic activity. These results provide structural insight into the different catalytic mechanisms of the two CESHs.