Hexa-N-acetylchitohexaose
(Synonyms: N,N',N,N''',N'''',N'''''-六乙酰壳六糖,N-Acetylchitohexaose，NACOS-6) 目录号 : GC43822
A hexamer of N-acetylglucosamine
Cas No.:38854-46-5
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Hexa-N-acetylchitohexaose is a hexamer of N-acetylglucosamine, a subunit of the natural polymer chitin. It functions as an elicitor in plants, inducing the expression of chitinases. [1][2] Like chitin and some of its derivatives, hexa-N-acetylchitohexaose is a substrate of lysozyme.[3] It also binds LysM domains on certain proteins, including an endopeptidase of T. thermophilus [4]. Hexa-N-acetylchitohexaose heightens the immune response against Pseudomonas and Listeria in mice, stimulates cytokine secretion in mesenchymal stem cells, and inhibits nitric oxide production by activated macrophages.[5][6][7][8]
Reference:
[1]. Inui, H., Yamaguchi, Y., and Hirano, S. Elicitor actions of N-acetylchitooligosaccharides and laminarioligosaccharides for chitinase and L-phenylalanine ammonia-lyase induction in rice suspension culture. Bioscience, Biotechnology, and Biochemistry 61(6), 975-978 (1997).
[2]. Gao, Y., Zan, X.L., Wu, X.F., et al. Identification of fungus-responsive cis-acting element in the promoter of Brassica juncea chitinase gene, BjCHI1. Plant Science 215-216, 190-198 (2014).
[3]. Ouyang, Z., Takáts, Z., Blake, T.A., et al. Preparing protein microarrays by soft-landing of mass-selected ions. Science 301, 1351-1354 (2003).
[4]. Wong, J.E.M.M., Midtgaard, S.R., Gysel, K., et al. An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. Acta.Cryst. D71, 592-605 (2014).
[5]. Tokoro, A., Kobayashi, M., Tatewaki, N., et al. Protective effect of N-acetyl chitohexaose on Listeria monocytogenes infection in mice. Microbiology and Immunology 33(4), 357-367 (1989).
[6]. Okawa, Y., Kobayashi, M., Suzuki, S., et al. Comparative study of protetive effects of chitin, chitosan, and N-acetyl chitohexaose against Pseudomonas aeruginosa and Listeria monocytogenes infections in mice. Biological and Pharmaceutical Bullentin 26(6), 902-904 (2003).
[7]. Lieder, R., Thormodsson, F., Ng, C.H., et al. Chitosan and chitin hexamers affect expansion and differentiation of mesenchymal stem cells differently. Int.J.Biol.Macromol. 51(4), 675-680 (2012).
[8]. Hwang, S.M., Chen, C.Y., Chen, S.S., et al. Chitinous materials inhibit nitric oxide production by activated RAW 264.7 macrophages. Biochemical and Biophysical Research Communications 271(1), 229-233 (2000).
| Cas No. | 38854-46-5 | SDF | |
| 别名 | N,N',N,N''',N'''',N'''''-六乙酰壳六糖,N-Acetylchitohexaose，NACOS-6 | ||
| 化学名 | O-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl-(1→4-O-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl-(1→4)-O-2-(acetylamino)-2-deoxy-β-D-glucopyranosy-(1→4)-O-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl-(1→4)-O-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl-(1→4)-2-(acetylamino)-2-deoxy-D-glucose | ||
| Canonical SMILES | OC[C@H]1O[C@](O[C@@H]2[C@@H](CO)O[C@](O[C@H]3[C@H](O)[C@@H](NC(C)=O)[C@H](O[C@]4([H])[C@@H](CO)O[C@@H](O[C@@]5([H])[C@H](O)[C@@H](NC(C)=O)[C@H](O[C@@]([C@H](O)CO)([H])[C@H](O)[C@@H](NC(C)=O)C=O)O[C@@H]5CO)[C@H](NC(C)=O)[C@H]4O)O[C@@H]3CO)([H])[C@H](N | ||
| 分子式 | C48H80N6O31 | 分子量 | 1237.2 |
| 溶解度 | 10mg/mL in PBS, pH 7.2 | 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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 0.8083 mL | 4.0414 mL | 8.0828 mL |
| 5 mM | 0.1617 mL | 0.8083 mL | 1.6166 mL |
| 10 mM | 0.0808 mL | 0.4041 mL | 0.8083 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。
An NMR and MD study of complexes of bacteriophage lambda lysozyme with tetra- and Hexa-N-acetylchitohexaose
Proteins 2020 Jan;88(1):82-93.PMID:31294851DOI:10.1002/prot.25770.
The X-ray structure of lysozyme from bacteriophage lambda (λ lysozyme) in complex with the inhibitor Hexa-N-acetylchitohexaose (NAG6) (PDB: 3D3D) has been reported previously showing sugar units from two molecules of NAG6 bound in the active site. One NAG6 is bound with four sugar units in the ABCD sites and the other with two sugar units in the E'F' sites potentially representing the cleavage reaction products; each NAG6 cross links two neighboring λ lysozyme molecules. Here we use NMR and MD simulations to study the interaction of λ lysozyme with the inhibitors NAG4 and NAG6 in solution. This allows us to study the interactions within the complex prior to cleavage of the polysaccharide. 1 HN and 15 N chemical shifts of λ lysozyme resonances were followed during NAG4/NAG6 titrations. The chemical shift changes were similar in the two titrations, consistent with sugars binding to the cleft between the upper and lower domains; the NMR data show no evidence for simultaneous binding of a NAG6 to two λ lysozyme molecules. Six 150 ns MD simulations of λ lysozyme in complex with NAG4 or NAG6 were performed starting from different conformations. The simulations with both NAG4 and NAG6 show stable binding of sugars across the D/E active site providing low energy models for the enzyme-inhibitor complexes. The MD simulations identify different binding subsites for the 5th and 6th sugars consistent with the NMR data. The structural information gained from the NMR experiments and MD simulations have been used to model the enzyme-peptidoglycan complex.
Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with Hexa-N-acetylchitohexaose
Biochemistry 2001 May 15;40(19):5665-73.PMID:11341831DOI:10.1021/bi0028035.
The three-dimensional structure of the lytic transglycosylase from bacteriophage lambda, also known as bacteriophage lambda lysozyme, complexed to the hexasaccharide inhibitor, Hexa-N-acetylchitohexaose, has been determined by X-ray crystallography at 2.6 A resolution. The unit cell contains two molecules of the lytic transglycosylase with two hexasaccharides bound. Each enzyme molecule is found to interact with four N-acetylglucosamine units from one hexasaccharide (subsites A-D) and two N-acetylglucosamine units from the second hexasaccharide (subsites E and F), resulting in all six subsites of the active site of this enzyme being filled. This crystallographic structure, therefore, represents the first example of a lysozyme in which all subsites are occupied, and detailed protein-oligosaccharide interactions are now available for this bacteriophage lytic transglycosylase. Examination of the active site furthermore reveals that of the two residues that have been implicated in the reaction mechanism of most other c-type lysozymes (Glu35 and Asp52 in hen egg white lysozyme), only a homologous Glu residue is present. The lambda lytic transglycosylase is therefore functionally closely related to the Escherichia coli Slt70 and Slt35 lytic transglycosylases and goose egg white lysozyme which also lack the catalytic aspartic acid.
Access to N-Acetylated Chitohexaose with Well-Defined Degrees of Acetylation
Biomed Res Int 2017;2017:2486515.PMID:28656139DOI:10.1155/2017/2486515.
Chitohexaose has attracted wide interest due to its special bioactivities and these potential activities are significantly related to N-acetylation. Herein, six chitohexaose fractions with different degrees of acetylation were prepared by selective N-acetylation and ion-exchange chromatography and further analyzed by ESI/MS. It is revealed that all the six N-acetylated chitohexaoses were of single molecular weight, the molecular weights of which were exactly assigned to 1026.44 Da, 1068.44 Da, 1110.48 Da, 1152.48 Da, 1194.49 Da, and 1236.48 Da, respectively. These results suggested that the six prepared N-acetylated chitohexaoses were N-acetylchitohexaose (D5A1), di-N-acetylchitohexaose (D4A2), tri-N-acetylchitohexaose (D3A3), tetra-N-acetylchitohexaose (D2A4), penta-N-acetylchitohexaose (D1A5), and Hexa-N-acetylchitohexaose (A6), respectively, which are of great significance to screen their bioactivities and discover well-defined chitooligosaccharide molecules as potential drugs.
TraG encoded by the pIP501 type IV secretion system is a two-domain peptidoglycan-degrading enzyme essential for conjugative transfer
J Bacteriol 2013 Oct;195(19):4436-44.PMID:23913323DOI:10.1128/JB.02263-12.
pIP501 is a conjugative broad-host-range plasmid frequently present in nosocomial Enterococcus faecalis and Enterococcus faecium isolates. We focus here on the functional analysis of the type IV secretion gene traG, which was found to be essential for pIP501 conjugative transfer between Gram-positive bacteria. The TraG protein, which localizes to the cell envelope of E. faecalis harboring pIP501, was expressed and purified without its N-terminal transmembrane helix (TraGΔTMH) and shown to possess peptidoglycan-degrading activity. TraGΔTMH was inhibited by specific lytic transglycosylase inhibitors Hexa-N-acetylchitohexaose and bulgecin A. Analysis of the TraG sequence suggested the presence of two domains which both could contribute to the observed cell wall-degrading activity: an N-terminal soluble lytic transglycosylase domain (SLT) and a C-terminal cysteine-, histidine-dependent amidohydrolases/peptidases (CHAP) domain. The protein domains were expressed separately, and both degraded peptidoglycan. A change of the conserved glutamate residue in the putative catalytic center of the SLT domain (E87) to glycine resulted in almost complete inactivity, which is consistent with this part of TraG being a predicted lytic transglycosylase. Based on our findings, we propose that TraG locally opens the peptidoglycan to facilitate insertion of the Gram-positive bacterial type IV secretion machinery into the cell envelope.
Enzymic synthesis of useful chito-oligosaccharides utilizing transglycosylation by chitinolytic enzymes in a buffer containing ammonium sulfate
Carbohydr Res 1990 Aug 1;203(1):65-77.PMID:2224904DOI:10.1016/0008-6215(90)80046-6.
A chitinase purified from culture filtrates of Trichoderma resei KDR-11 efficiently catalyzed a transglycosylation reaction on tetra-N-acetylchitotetraoside in a buffer medium containing ammonium sulfate, converting the tetrasaccharide into Hexa-N-acetylchitohexaose (39.6%) and di-N-acetylchitobiose (55.7%) as the major products. Sugar-chain elongation from di-N-acetylchitobiose as the initial substrate to hexa-N-acetyl-chitohexaose and hepta-N-acetylchitoheptaose was also efficiently induced through lysozyme catalysis in the presence of ammonium sulfate at high (30%) concentration. In this case, the addition of ammonium sulfate to the reaction system resulted in a remarkable increase of the hexamer and heptamer productions, which are desirable as biologically active oligosaccharides.