L-aminoadipate semialdehyde | 73980-78-6

• 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
• 英文名称: L-aminoadipate semialdehyde
• 英文别名: L-Δ¹-piperideine-6-carboxylic acid；piperideine-6-carboxylic acid；L-AASA；(2S)-2,3,4,5-tetrahydropyridin-1-ium-2-carboxylate
• CAS: 73980-78-6
• 化学式: C₆H₉NO₂
• 分子量: 127.143
• InChiKey: CSDPVAKVEWETFG-YFKPBYRVSA-N

物化性质

• 沸点：
  309.0±42.0 °C(Predicted)
• 密度：
  1.27±0.1 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  9
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  49.7
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  L-aminoadipate semialdehyde 在 水 作用下， 生成 L-赖氨酸
  参考文献：
  名称：

  重建关键微域的自然进化趋势为热微生物 N-去甲基酶的工程设计提供了有效策略

  摘要：

  据报道， N-去甲基化酶可以去除伯胺或仲胺上的甲基，这可能会进一步影响生物大分子或化合物的性质和功能；然而，尚未系统地研究N-去甲基化酶的底物范围和稳健性。在这里，我们报告了Thermomicrobium roseum肌氨酸氧化酶 (TrSOX) 关键微域中自然进化的再现，这是一种N-脱甲基酶具有显着的稳定性（熔化温度超过 100 °C）和对映选择性，可增强底物范围和对 -CN- 键的催化效率。对于初始框架，我们通过结晶和 X 射线衍射 (XRD) 获得了 TrSOX 的结构。然后使用祖先序列重建 (ASR) 识别关键微结构域的非保守残基（包括催化环、辅酶口袋、底物口袋和入口位点）的自然进化，并通过位点重建自然进化过程中产生的替换。定向诱变。单取代和双取代变体催化N的N-去甲基化-甲基-L-氨基酸分别比野生型快 1800 倍和 6000 倍。此外，这些单取代变体催化了非氨基酸化合物的末端N

  DOI：

  10.1016/j.jbc.2022.101656
• 作为产物：
  描述：

  L-赖氨酸 在 磷酸吡哆醛 、 transaminase from Halomonas elongata 、 丙酮酸 、 还原型辅酶Ⅰ 作用下， 以 aq. phosphate buffer 为溶剂， 生成 L-aminoadipate semialdehyde
  参考文献：
  名称：

  Cell-free biocatalytic syntheses of l-pipecolic acid: a dual strategy approach and process intensification in flow

  摘要：

  作为传统化学合成或体内生产l-吡嗪酸的替代方案，我们开发了两种使用纯化和固定酶的外体策略，用于生产这一关键构建模块。

  DOI：

  10.1039/d0gc01817a

文献信息

• Stereoselective preparation of lipidated carboxymethyl-proline/pipecolic acid derivatives via coupling of engineered crotonases with an alkylmalonyl-CoA synthetase
  作者：Refaat B. Hamed、Luc Henry、J. Ruben Gomez-Castellanos、Amina Asghar、Jürgen Brem、Timothy D. W. Claridge、Christopher J. Schofield

  DOI：10.1039/c3ob41525b

  日期：——

  The trisubstituted enolate- and C–C bond-forming capacities of engineered carboxymethylproline synthases CMPSs are coupled with the malonyl-CoA synthetase MatB to enable stereoselective preparation of 5- and 6-membered N-heterocycles functionalised with alkyl-substituted carboxymethyl side chains, starting from achiral alkyl-substituted malonic acids and L-amino acid semialdehydes. The results illustrate the biocatalytic utility of crotonases in tandem enzyme-catalysed reactions for stereoselective synthesis.

  工程化羧甲基脯氨酸合酶（CMPS）具有三取代烯醇化和C-C键形成能力，与丙二酰-CoA合成酶MatB偶联，可实现从非手性烷基取代的丙二酸和L-氨基酸半醛出发，选择性制备带有烷基取代羧甲基侧链的5-和6-元N-杂环。这些结果展示了利用裂解酶在串联酶催化反应中进行选择性合成生物催化的实用性。
• Stereoselective C–C bond formation catalysed by engineered carboxymethylproline synthases
  作者：Refaat B. Hamed、J. Ruben Gomez-Castellanos、Armin Thalhammer、Daniel Harding、Christian Ducho、Timothy D. W. Claridge、Christopher J. Schofield

  DOI：10.1038/nchem.1011

  日期：2011.5

  enabling stereoselective C–C bond formation leading to N-heterocycles via control of trisubstituted enolate intermediates. Active site substitutions, including at the oxyanion binding site, enable the production of substituted N-heterocycles in high diastereomeric excesses via stereocontrolled enolate formation and reaction. The results reveal the potential of the ubiquitous crotonase superfamily as

  烯醇（酸酯）与亲电试剂的反应广泛用于有机合成中，用于立体选择性 C-C 键的形成。基于蛋白质的催化剂在通过烯醇化物化学选择性形成 C-C 键的立体选择性形成方面的应用相对有限。我们描述了对巴豆酶超家族成员 5-羧甲基脯氨酸合酶的蛋白质工程研究，旨在通过控制三取代的烯醇中间体来实现立体选择性 C-C 键形成，从而产生N-杂环。活性位点取代，包括氧阴离子结合位点，能够产生取代的N-通过立体控制的烯醇化物形成和反应产生高非对映体过量的杂环。结果揭示了普遍存在的巴豆糖酶超家族作为控制烯醇化物化学的适应性催化剂的潜力。
• Nitrilases, Nucleic Acids Encoding Them and Methods for Making and Using Them
  申请人：DeSantis Grace

  公开号：US20100273659A1

  公开（公告）日：2010-10-28

  The invention relates to nitrilases and to nucleic acids encoding the nitrilases. In addition methods of designing new nitrilases and method of use thereof are also provided. The nitrilases have increased activity and stability at increased pH and temperature.

  本发明涉及腈水解酶及编码腈水解酶的核酸。此外，还提供了设计新腈水解酶的方法和使用它们的方法。这些腈水解酶在高pH和高温下具有增强的活性和稳定性。
• Structural and biochemical consequences of pyridoxine‐dependent epilepsy mutations that target the aldehyde binding site of aldehyde dehydrogenase <scp>ALDH</scp> 7A1
  作者：Adrian R. Laciak、David A. Korasick、Jesse W. Wyatt、Kent S. Gates、John J. Tanner

  DOI：10.1111/febs.14997

  日期：2020.1

  In humans, certain mutations in the gene encoding aldehyde dehydrogenase 7A1 are associated with pyridoxine‐dependent epilepsy (PDE). Understanding the impact of PDE‐causing mutations on the structure and activity of ALDH7A1 could allow for the prediction of symptom‐severity and aid the development of patient‐specific medical treatments. Herein, we investigate the biochemical and structural consequences of PDE missense mutations targeting residues in the aldehyde substrate binding site: N167S, P169S, A171V, G174V, and W175G. All but G174V could be purified for biochemical and X‐ray crystallographic analysis. W175G has a relatively mild kinetic defect, exhibiting a fivefold decrease in kcat with no change in Km. P169S and N167S have moderate defects, characterized by catalytic efficiencies of 20‐ and 100‐times lower than wild‐type, respectively. A171V has a profound functional defect, with catalytic efficiency 2000‐times lower than wild‐type. The crystal structures of the variants are the first for any PDE‐associated mutant of ALDH7A1. The structures show that missense mutations that decrease the steric bulk of the side chain tend to create a cavity in the active site. The protein responds by relaxing into the vacant space, and this structural perturbation appears to cause misalignment of the aldehyde substrate in W175G and N167S. The P169S structure is nearly identical to that of the wild‐type enzyme; however, analysis of B‐factors suggests the catalytic defect may result from altered protein dynamics. The A171V structure suggests that the potential for steric clash with Val171 prevents Glu121 from ion pairing with the amino group of the aldehyde substrate.EnzymesAldehyde dehydrogenase 7A1 (EC1.2.1.31).DatabasesCoordinates have been deposited in the Protein Data Bank under the following accession codes: 6O4B, 6O4C, 6O4D, 6O4E, 6O4F, 6O4G, 6O4H.
• PROCESS FOR THE BIOLOGICAL PRODUCTION OF L-PIPECOLIC ACID
  申请人：MERCIAN CORPORATION

  公开号：EP1249494B1

  公开（公告）日：2009-02-18