L-Fucitol
(Synonyms: L-岩藻糖醇,1-Deoxy-D-galactitol) 目录号 : GC38427
A reduced form of L-(–)-fucose
Cas No.:13074-06-1
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
L-Fucitol is a reduced form of L-(–)-fucose . It has been used to determine the structure of E. coli and B. pallidus L-fucose isomerase.1,2
1.Seemann, J.E., and Schulz, G.E.Structure and mechanism of L-fucose isomerase from Escherichia coliJ. Mol. Biol.273(1)256-268(1997) 2.Takeda, K., Yoshida, H., Izumori, K., et al.X-ray structures of Bacillus pallidus D-arabinose isomerase and its complex with L-fucitolBiochim. Biophys. Acta1804(6)1359-1368(2010)
| Cas No. | 13074-06-1 | SDF | |
| 别名 | L-岩藻糖醇,1-Deoxy-D-galactitol | ||
| Canonical SMILES | C[C@@H]([C@H]([C@H]([C@@H](CO)O)O)O)O | ||
| 分子式 | C6H14O5 | 分子量 | 166.17 |
| 溶解度 | Water: 125 mg/mL (752.24 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 | 6.0179 mL | 30.0897 mL | 60.1793 mL |
| 5 mM | 1.2036 mL | 6.0179 mL | 12.0359 mL |
| 10 mM | 0.6018 mL | 3.009 mL | 6.0179 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。
1-De-oxy-d-galactitol (L-Fucitol)
Acta Crystallogr Sect E Struct Rep Online 2008 Jul 9;64(Pt 8):o1429.PMID:21203146DOI:10.1107/S1600536808020345.
1-De-oxy-d-galactitol, C(6)H(14)O(5), exists in the crystalline form as hydrogen-bonded layers of mol-ecules running parallel to the ac plane, with each mol-ecule acting as a donor and acceptor of five hydrogen bonds.
X-ray structures of Bacillus pallidus d-arabinose isomerase and its complex with L-Fucitol
Biochim Biophys Acta 2010 Jun;1804(6):1359-68.PMID:20123133DOI:10.1016/j.bbapap.2010.01.018.
d-Arabinose isomerase (d-AI), also known as l-fucose isomerase (l-FI), catalyzes the aldose-ketose isomerization of d-arabinose to d-ribulose, and l-fucose to l-fuculose. Bacillus pallidus (B. pallidus) d-AI can catalyze isomerization of d-altrose to d-psicose, as well as d-arabinose and l-fucose. Three X-ray structures of B. pallidus d-AI in complexes with 2-methyl-2,4-pentadiol, glycerol and an inhibitor, L-Fucitol, were determined at resolutions of 1.77, 1.60 and 2.60 A, respectively. B. pallidus d-AI forms a homo-hexamer, and one subunit has three domains of almost equal size; two Rossmann fold domains and a mimic of the (beta/alpha) barrel fold domain. A catalytic metal ion (Mn(2+)) was found in the active site coordinated by Glu342, Asp366 and His532, and an additional metal ion was found at the channel for the passage of a substrate coordinated by Asp453. The X-ray structures basically supported the ene-diol mechanism for the aldose-ketose isomerization by B. pallidus d-AI, as well as Escherichia coli (E. coli) l-FI, in which Glu342 and Asp366 facing each other at the catalytic metal ion transfer a proton from C2 to C1 and O1 to O2, acting as acid/base catalysts, respectively. However, considering the ionized state of Asp366, the catalytic reaction also possibly occurs through the negatively charged ene-diolate intermediate stabilized by the catalytic metal ion. A structural comparison with E. colil-FI showed that B. pallidus d-AI possibly interconverts between "open" and "closed" forms, and that the additional metal ion found in B. pallidus d-AI may help to stabilize the channel region.
Facile synthesis of sulfonium ion derivatives of 1,5-anhydro-5-thio-L-fucitol as potential alpha-L-fucosidase inhibitors
Carbohydr Res 2006 Nov 6;341(15):2478-86.PMID:16930571DOI:10.1016/j.carres.2006.08.002.
Five sulfonium ion derivatives with 1,5-anhydro-5-thio-L-fucitol as a core structure were efficiently synthesized as potential alpha-L-fucosidase inhibitors. The key unit, the tri-O-benzyl derivative of L-Fucitol, was readily synthesized from methyl alpha-D-mannopyranoside. Alkylation with methyl iodide or 5-methoxycarbonyl-1-pentyl iodide in acetonitrile containing AgBF4 afforded the corresponding alkylated sulfonium tetrafluoroborates. Alternatively, ring opening of three 1,3-cyclic sulfates in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) containing K2CO3 afforded the corresponding zwitterionic sulfonium sulfates.
Structure and mechanism of L-fucose isomerase from Escherichia coli
J Mol Biol 1997 Oct 17;273(1):256-68.PMID:9367760DOI:10.1006/jmbi.1997.1280.
The three-dimensional structure of L-fucose isomerase from Escherichia coli has been determined by X-ray crystallography at 2.5 A resolution. This ketol isomerase converts the aldose L-fucose into the corresponding ketose L-fuculose using Mn2+ as a cofactor. Being a hexamer with 64,976 Da per subunit, L-fucose isomerase is the largest structurally known ketol isomerase. The enzyme shows neither sequence nor structural similarity with other ketol isomerases. The hexamer obeys D3 symmetry and forms the crystallographic asymmetric unit. The strict and favorably oriented local symmetry allowed for a computational phase extension from 7.3 A to 2.5 A resolution. The structure was solved with an L-Fucitol molecule bound to the catalytic center such that the hydroxyl groups at positions 1 and 2 are ligands of the manganese ion. Most likely, L-Fucitol mimics a bound L-fucose molecule in its open chain form. The protein environment suggests strongly that the reaction belongs to the ene-diol type.
A mutant inducible for galactitol utilization in Escherichia coli K12
J Gen Microbiol 1982 Mar;128(3):601-4.PMID:7042910DOI:10.1099/00221287-128-3-601.
Galactitol-positive strains of Escherichia coli K12 are inhibited by the galactitol analogues L-Fucitol and 2-deoxy-D-galactitol, but not by D-fucitol; Salmonella typhimurium LT2 is not inhibited by these compounds. Most mutants selected as resistant to either toxic compound are unable to utilize galactitol as carbon source, but a relatively rare class is inducible for the Enzyme II of the galactitol:phosphoenolpyruvate phosphotransferase system, the product of which is D-galactitol 6-phosphate. The lesion in one such mutant maps near metG at about min 45 on the E. coli genome.