(6S,2S)-二氨基庚二酸 | 14289-34-0

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 中文名称: (6S,2S)-二氨基庚二酸
• 英文名称: (S,S)-2,6-diaminopimelic acid
• 英文别名: (2S,6S)-2,6-diaminoheptanedioic acid；(2S,6S)-(+)-2,6-diaminopimelic acid；(2S,6S)-(+)-diaminopimelic acid；(2S,6S)-2,6-diaminopimelic acid；L-2,6-diaminoheptanedioic acid；L,L-2,6-diaminopimelic acid；(2S,6S)-2,6-diaminoheptanedioate；(2S,6S)-2,6-bis(azaniumyl)heptanedioate
• CAS: 14289-34-0
• 化学式: C₇H₁₄N₂O₄
• 分子量: 190.199
• InChiKey: GMKMEZVLHJARHF-WHFBIAKZSA-N

物化性质

• 沸点：
  426.7±45.0 °C(Predicted)
• 密度：
  1.344±0.06 g/cm3(Predicted)
• 熔点：
  309-312 °C
• 物理描述：
  Solid
• 碰撞截面：
  140.02 Ų [M-H]- [CCS Type: DT, Method: stepped-field]

计算性质

• 辛醇/水分配系数(LogP)：
  -5.9
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  127
• 氢给体数：
  4
• 氢受体数：
  6

安全信息

• 海关编码：
  2922499990
• 储存条件：
  | 室温 |

反应信息

• 作为反应物：
  描述：

  (6S,2S)-二氨基庚二酸 在 potassium hydrogencarbonate 、 三氟乙酸 作用下， 以 乙醇 、 水 为溶剂， 反应 2.0h， 生成 (2S,6S)-2-Amino-6-((S)-2-amino-propionylamino)-heptanedioic acid
  参考文献：
  名称：

  Peptides of 2-aminopimelic acid: antibacterial agents that inhibit diaminopimelic acid biosynthesis

  摘要：

  Succinyl-CoA:tetrahydrodipicolinate-N-succinyltransferase is a key enzyme in the biosynthesis of diaminopimelic acid (DAP), a component of the cell wall peptidoglycan of nearly all bacteria. This enzyme converts the cyclic precursor tetrahydrodipicolinic acid (THDPA) to a succinylated acyclic product. L-2-Aminopimelic acid (L-1), an acyclic analogue of THDPA, was found to be a good substrate for this enzyme and was shown to cause a buildup of THDPA in a cell-free enzyme system but was devoid of antibacterial activity. Incorporation of 1 into a di- or tripeptide yielded derivatives that exhibited antibacterial activity against a range of Gram-negative organisms. Of the five peptide derivatives tested, (L-2-aminopimelyl)-L-alanine (6) was the most potent. These peptides were shown to inhibit DAP production in intact resting cells. High levels (30 mM) of 2-aminopimelic acid were achieved in the cytoplasm of bacteria as a result of efficient uptake of the peptide derivatives through specific peptide transport systems followed, presumably, by cleavage by intracellular peptidases. Finally, the antibacterial activity of these peptides could be reversed by DAP or a DAP-containing peptide. These results demonstrate that the peptides containing L-2-aminopimelic acid exert their antibacterial action by inhibition of diaminopimelic acid biosynthesis.

  DOI：

  10.1021/jm00151a015
• 作为产物：
  描述：

  tert-butyl (2S)-2-{bis[(tert-butoxy)carbonyl]amino}-5-oxopentanoate 在 [(1,2,5,6-r)-1,5-cyclooctadiene][(2S,2'S,5 S,5'S)-1,1'-(1,2-phenylene)bis[2,5-diethylphospholane-κP]]-rhodium(1+) trifluoromethanesulfonate 氢溴酸 、 氢气 、 溶剂黄146 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 苯酚 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 20.0 ℃ 、482.63 kPa 条件下， 反应 44.5h， 生成 (6S,2S)-二氨基庚二酸
  参考文献：
  名称：

  通过不对称氢化高效合成 (2S,6S)- 和内消旋二氨基庚二酸

  摘要：

  已成功开发了标题化合物 1 和 2 的有效合成方法。关键步骤是使用 [Rh(I)(COD)-(S,S) 或 -(R,R)-Et-DuPHOS)] + OTf 对脱氢氨基酸 7 进行不对称氢化，以产生具有光学活性的受保护氨基酸高 ee (>95%) 的衍生物 该方法还可用于合成其他异构体和类似物。

  DOI：

  10.1055/s-2002-19295

文献信息

• Synthesis of bis-α,α′-amino acids through diastereoselective bis-alkylations of chiral Ni(ii)-complexes of glycine
  作者：Jiang Wang、Hong Liu、José Luis Aceña、Daniel Houck、Ryosuke Takeda、Hiroki Moriwaki、Tatsunori Sato、Vadim A. Soloshonok

  DOI：10.1039/c3ob40594j

  日期：——

  conditions for the alkylation reactions have been investigated and the latter proved to be more efficient in terms of stereochemical outcome. In particular, alkylation of the glycine Schiff base Ni(II) complex with 1,3-dibromopropane followed by acid-catalysed hydrolysis of the resulting bis-alkylation product, allowed for the preparation of naturally occurring (2S,6S)-diaminopimelic acid in high overall

  Ni（II）络合物衍生自甘氨酸 希夫基地 （S）-N-（苄基脯氨酰基）-2-氨基二苯甲酮可用α，ω-二溴化物试剂有效地烷基化以提供相应的双烷基化产物。该方法提供了制备具有高生物学重要性的相应双-α，α'-氨基酸的直接方法。已经研究了烷基化反应的非均相（相转移）条件和均相条件，事实证明后者在立体化学结果方面更为有效。特别是，甘氨酸席夫碱Ni（II）配合物的烷基化1,3-二溴丙烷 然后将所得的双烷基化产物进行酸催化水解，从而可以制备天然存在的 （2 S，6 S）-二氨基庚二酸 总产量高。
• Synthesis of characteristic Mycobacterium peptidoglycan (PGN) fragments utilizing with chemoenzymatic preparation of meso-diaminopimelic acid (DAP), and their modulation of innate immune responses
  作者：Qianqian Wang、Yusuke Matsuo、Ambara R. Pradipta、Naohiro Inohara、Yukari Fujimoto、Koichi Fukase

  DOI：10.1039/c5ob02145f

  日期：——

  CharacteristicMycobacteriumpeptidoglycan fragments were comprehensively synthesized and their weaker immunostimulationviaNod1 and Nod2 was shown.

  特征性的分子Mycobacterium肽聚糖片段已全面合成，并显示了它们通过Nod1和Nod2较弱的免疫刺激作用。
• Atomic-Resolution 1.3 Å Crystal Structure, Inhibition by Sulfate, and Molecular Dynamics of the Bacterial Enzyme DapE
  作者：Matthew Kochert、Boguslaw P. Nocek、Thahani S. Habeeb Mohammad、Elliot Gild、Kaitlyn Lovato、Tahirah K. Heath、Richard C. Holz、Kenneth W. Olsen、Daniel P. Becker

  DOI：10.1021/acs.biochem.0c00926

  日期：2021.3.30

  We report the atomic-resolution (1.3 Å) X-ray crystal structure of an open conformation of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE, EC 3.5.1.18) from Neisseria meningitidis. This structure [Protein Data Bank (PDB) entry 5UEJ] contains two bound sulfate ions in the active site that mimic the binding of the terminal carboxylates of the N-succinyl-l,l-diaminopimelic acid (l,l-SDAP) substrate. We demonstrated inhibition of DapE by sulfate (IC50 = 13.8 ± 2.8 mM). Comparison with other DapE structures in the PDB demonstrates the flexibility of the interdomain connections of this protein. This high-resolution structure was then utilized as the starting point for targeted molecular dynamics experiments revealing the conformational change from the open form to the closed form that occurs when DapE binds l,l-SDAP and cleaves the amide bond. These simulations demonstrated closure from the open to the closed conformation, the change in RMS throughout the closure, and the independence in the movement of the two DapE subunits. This conformational change occurred in two phases with the catalytic domains moving toward the dimerization domains first, followed by a rotation of catalytic domains relative to the dimerization domains. Although there were no targeting forces, the substrate moved closer to the active site and bound more tightly during the closure event.

  我们报告了脑膜炎奈瑟菌中由 dapE 编码的 N-琥珀酰-l,l-二氨基亚庚酸脱琥珀酰化酶（DapE，EC 3.5.1.18）的开放构象的原子分辨率（1.3 Å）X 射线晶体结构。该结构[蛋白质数据库（PDB）条目 5UEJ]的活性位点含有两个结合的硫酸根离子，模拟 N-琥珀酰-l,l-二氨基亚庚酸（l,l-SDAP）底物末端羧酸根的结合。我们证实了硫酸盐对 DapE 的抑制作用（IC50 = 13.8 ± 2.8 mM）。与 PDB 中其他 DapE 结构的比较显示了该蛋白结构域间连接的灵活性。随后，以这一高分辨率结构为起点，进行了有针对性的分子动力学实验，揭示了当 DapE 结合 l,l-SDAP 并裂解酰胺键时，从开放形态到封闭形态的构象变化。这些模拟展示了从开放构象到封闭构象的闭合、整个闭合过程中 RMS 的变化以及两个 DapE 亚基运动的独立性。这种构象变化分为两个阶段，首先是催化结构域向二聚结构域移动，然后是催化结构域相对于二聚结构域的旋转。虽然没有靶向力，但底物在闭合过程中更靠近活性位点，结合得更紧密。
• Stereoselektive Synthese von (2<i>S</i>,6<i>S</i>)-2,6-Diaminoheptandisäure und von unsymmetrischen Derivaten der<i>meso</i>-2,6-Diaminoheptandisäure
  作者：Guido Bold、Thomas Allmendinger、Peter Herold、Luzia Moesch、Hans-Peter Schär、Rudolf O. Duthaler

  DOI：10.1002/hlca.19920750321

  日期：1992.5.6

  Stereoselective Synthesis of (2S,6S)-2,6-Diaminoheptanedioic Acid and of Unsymmetrical Derivatives of meso-2,6-Diaminoheptanedioic Acid

  （2 S，6 S）-2,6-二氨基庚二酸和内消旋-2,6-二氨基庚二酸的不对称衍生物的立体选择性合成
• Crystal Structure of ll-Diaminopimelate Aminotransferase from Arabidopsis thaliana: A Recently Discovered Enzyme in the Biosynthesis of l-Lysine by Plants and Chlamydia
  作者：Nobuhiko Watanabe、Maia M. Cherney、Marco J. van Belkum、Sandra L. Marcus、Mitchel D. Flegel、Matthew D. Clay、Michael K. Deyholos、John C. Vederas、Michael N.G. James

  DOI：10.1016/j.jmb.2007.05.061

  日期：2007.8

  inhibitors, the three-dimensional crystal structure of LL-DAP-AT was determined at 1.95 A resolution. The cDNA sequence of LL-DAP-AT from Arabidopsis thaliana (AtDAP-AT) was optimized for expression in bacteria and cloned in Escherichia coli without its leader sequence but with a C-terminal hexahistidine affinity tag to aid protein purification. The structure of AtDAP-AT was determined using the multiple-wavelength

  细菌和植物中赖氨酸赖氨酸的基本生物合成途径是开发新型抗生素或除草剂的有吸引力的目标，因为人类中不存在这种赖氨酸，必须在饮食中获取该氨基酸。植物使用细菌通往L-赖氨酸的捷径，其中依赖吡al醛5'-磷酸（PLP）的酶ll-二氨基庚二酸酯氨基转移酶（LL-DAP-AT）将L-四氢二吡啶甲酸（L-THDP）直接转化为LL-DAP。此外，最近在衣原体中发现了LL-DAP-AT，这表明该酶的抑制剂也可能有效对抗这种生物。为了理解该酶的机理并协助抑制剂的设计，以1.95 A的分辨率确定了LL-DAP-AT的三维晶体结构。优化拟南芥LL-DAP-AT（AtDAP-AT）的cDNA序列，使其在细菌中表达，并克隆到大肠杆菌中而没有其前导序列，但具有C端六组氨酸亲和标签以帮助蛋白质纯化。使用硒代蛋氨酸衍生物的多波长异常色散（MAD）方法确定AtDAP-AT的结构。AtDAP-AT作为同型二聚体具有活性，每个亚基

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