(R)-3-Boc-氨基-γ-丁内酯 | 137105-97-6

• 物质功能分类: 化学试剂 - 有机试剂 - 酯类
• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 中文名称: (R)-3-Boc-氨基-γ-丁内酯
• 英文名称: (R)-4-(tert-butyloxycarbonylamino)-γ-butyrolactone
• 英文别名: tert-butyl (R)-(5-oxotetrahydrofuran-3-yl)carbamate；(R)-tert-Butyl (5-oxotetrahydrofuran-3-yl)carbamate；tert-butyl N-[(3R)-5-oxooxolan-3-yl]carbamate
• CAS: 137105-97-6
• 化学式: C₉H₁₅NO₄
• 分子量: 201.222
• InChiKey: XODLOLQRSQGSFE-ZCFIWIBFSA-N

物化性质

• 熔点：
  113-115 °C
• 沸点：
  363.7±31.0 °C(Predicted)
• 密度：
  1.15±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  14
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  64.6
• 氢给体数：
  1
• 氢受体数：
  4

安全信息

• 危险性防范说明：
  P264,P280,P302+P352,P305+P351+P338,P332+P313,P337+P313,P362
• 危险性描述：
  H315,H319

反应信息

• 作为反应物：
  描述：

  (R)-3-Boc-氨基-γ-丁内酯 在 吡啶 、 三甲基铝 、 mercury(II) trifluoroacetate 、 三乙胺 、 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 六甲基磷酰三胺 、 二氯甲烷 、 水 为溶剂， 生成 (4R,αR)-α-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid
  参考文献：
  名称：

  机械了解α-苄基-2-氧代-1,3-恶唑烷-4-乙酸使羧肽酶A失活，这是一种新型的不可逆性羧肽酶A抑制剂，没有立体特异性。

  摘要：

  根据羧肽酶A（CPA）的活性位点拓扑结构和酶催化机制，原型为含锌的蛋白水解酶，α-苄基-2-氧代-1,3-恶唑烷-4-乙酸（1）为被设计为一种新型的基于机制的酶灭活剂。从光学活性的天冬氨酸开始，以对映体纯的形式合成了抑制剂的所有四种可能的立体异构体，并对它们的CPA抑制活性进行了评估，发现令人惊讶的是，所有四种立体异构体均以时间依赖性方式抑制了CPA。透析后，抑制的酶没有恢复其酶活性。灭活被2-苄基琥珀酸阻止，后者是一种竞争性抑制剂，已知能与酶的活性位点结合。这些动力学结果强烈支持灭活剂在活性位点共价附于酶。对失活的CPA的ESI质谱数据进行分析，从动力学结果可以得出结论。二阶抑制率常数（k（obs）/ [I]（o））的值在1.7-3.6 M（-1）min（-1）的范围内。失活中缺乏立体定向性，导致我们提出环裂解是通过亲核攻击在2位而不是5位发生的，开环发生在加成消除机理中。认为该途径将产

  DOI：

  10.1021/jo010421e
• 作为产物：
  描述：

  二碳酸二叔丁酯 在 四丁基氟化铵 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 生成 (R)-3-Boc-氨基-γ-丁内酯
  参考文献：
  名称：

  Catalytic enantioselective synthesis of a novel inhibitor of ceramide trafficking, (1R,3R)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide (HPA-12)

  摘要：

  A novel inhibitor of ceramide trafficking, (1R,3R)-N-(3-hydroxy-1-hydroxymethyl-3-phenylpropyl)dodecanamide (HPA-12), has been synthesized using a chiral zirconium-catalyzed asymmetric Mannich-type reaction as a key-step. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4039(01)01658-6

文献信息

• Self-assembled ion-pair organocatalysis – asymmetric Baeyer–Villiger oxidation mediated by flavinium–cinchona alkaloid dimer
  作者：Pramod Prasad Poudel、Kenji Arimitsu、Kana Yamamoto

  DOI：10.1039/c6cc00663a

  日期：——

  An ion-pair catalyst generated by assembly of a chiral flavinium and a cinchona alkaloid dimer for use in asymmetric Baeyer-Villiger oxidation is presented.

  提出了通过手性黄酮和金鸡纳生物碱二聚体的组装产生的离子对催化剂，用于不对称的Baeyer-Villiger氧化。
• Isoindoline derivatives
  申请人：KYORIN PHARMACEUTICAL CO., LTD.

  公开号：EP0443498A1

  公开（公告）日：1991-08-28

  Optically active 8-methoxyquinolonecarboxylic acids represented by the formula (I) wherein R1 is lower alkyl have been found to possess potent antibacterial activity against both Gram-negative and Gram-positive bacteria. The compounds may be synthesized from novel optically active intermediates.

  光学活性的8-甲氧基喹啉羧酸（化学式为(I)，其中R1为低碳烷基）已被发现具有强大的抗细菌活性，对革兰氏阴性和革兰氏阳性细菌均有效。这些化合物可以从新颖的光学活性中间体合成。
• Revised Stereochemistry of Ceramide-Trafficking Inhibitor HPA-12 by X-ray Crystallography Analysis
  作者：Masaharu Ueno、Yi-Yong Huang、Akihito Yamano、Shu̅ Kobayashi

  DOI：10.1021/ol401101u

  日期：2013.6.7

  the stereochemistry of HPA-12, an important ceramide-trafficking inhibitor that was discovered and synthesized and its stereochemistry determined in 2001, the synthesis and the stereochemistry were reinvestigated. A large-scale synthetic method for HPA-12 based on a Zn-catalyzed asymmetric Mannich-type reaction in water was developed. Single crystals of HPA-12 for X-ray crystallographic analysis were

  响应伯克什（Berkeš）的报告，修改和合成了重要的神经酰胺贩运抑制剂HPA-12的立体化学，并于2001年确定了其立体化学，对此合成和立体化学进行了重新研究。提出了一种基于锌催化水中不对称曼尼希型反应的HPA-12大规模合成方法。由丙酸乙酯/获得用于X射线晶体学分析HPA-12的单晶Ñ己烷，和立体化学明确确定为1 - [R，3小号，与贝尔克斯订正结构一致。
• The synthesis of Fmoc-O-allyl β-serine
  作者：Ylva Bergman、Marisa Ciampini、Sania Jalal、Helen Rachel Lagiakos、Marie-Isabel Aguilar、Patrick Perlmutter

  DOI：10.1016/j.tetasy.2008.12.022

  日期：2008.12

  Two concise routes for the synthesis of the title amino acid have been developed. The first route employs Seebach's general approach [Seebach, D.; Lelais, G.; Micuch, P.; Josien-Lefebvre, D.; Rossi, F. Helv. Chim. Acta 2004, 87, 3131] with Arndt Eistert homologation of Boc-alpha-allyl alpha-serine as the key process. The second route employs an approach using Boc-alpha-aspartic acid as a starting material [Salzmann, T.N.; Ratcliffe, R.W.; Christensen, B.G.; Bouffard, F.A.J Am. Chem. Soc. 1980, 102, 6163; Rodriguez, M.; Llinares, M.; Doulut, S.; Heitz, A.; Martinez, J. Tetrahedron. Lett. 1991, 32, 923] with a selective palladium-catalysed O-allylation [Haight, A.R: Stoner, EJ.; Peterson, MJ.: Grover, V.K.J. Org. Chem. 2003, 68, 8092] as key processes. These two routes are evaluated for their relative efficiency and safety. (C) 2008 Elsevier Ltd. All rights reserved.
• Engineering of a Baeyer‐Villiger monooxygenase to Improve Substrate Scope, Stereoselectivity and Regioselectivity
  作者：Xu Li、Congcong Li、Ge Qu、Bo Yuan、Zhoutong Sun

  DOI：10.1002/cbic.202400328

  日期：2024.7.2

  Baeyer‐Villiger monooxygenases belong to a family of flavin‐binding proteins that catalyze the Baeyer‐Villiger (BV) oxidation of ketones to produce lactones or esters, which are important intermediates in pharmaceuticals or sustainable materials. Phenylacetone monooxygenase (PAMO) from Thermobifida fusca with moderate thermostability catalyzes the oxidation of aryl ketone substrates, but is limited by high specificity and narrow substrate scope. In the present study, we applied loop optimization by loop swapping followed by focused saturation mutagenesis in order to evolve PAMO mutants capable of catalyzing the regioselective BV oxidation of cyclohexanone and cyclobutanone derivatives with formation of either normal or abnormal esters or lactones. We further modulated PAMO to increase enantioselectivity. Crystal structure studies indicate that rotation occurs in the NADP‐binding domain and that the high B‐factor region is predominantly distributed in the catalytic pocket residues. Computational analyses further revealed dynamic character in the catalytic pocket and reshaped hydrogen bond interaction networks, which is more favorable for substrate binding. Our study provides useful insights for studying enzyme‐substrate adaptations.