D-酪氨酸苄酯 | 97984-62-8

• 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: D-酪氨酸苄酯
• 英文名称: (R)-benzyl 2-amino-3-(4-hydroxyphenyl)propanoate
• 英文别名: D-tyrosine benzyl ester；H-D-Tyr-OBn；D-Tyr-OBzl；D-Tyrosin-benzylester；benzyl (2R)-2-amino-3-(4-hydroxyphenyl)propanoate
• CAS: 97984-62-8
• 化学式: C₁₆H₁₇NO₃
• 分子量: 271.316
• InChiKey: BVCTWRNVKLXEQC-OAHLLOKOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  20
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  72.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  D-酪氨酸苄酯 生成 N-BOC-D-酪氨酸苄酯
  参考文献：
  名称：

  HIRAI, YOSHIRO;YOKOTA, KATSUYUKI;YAMAZAKI, TAKAO;NOMOSE, TAKEFUMI, HETEROCYCLES, 30,(1990) N, C. 1101-1119

  摘要：

  DOI：
• 作为产物：
  描述：

  D,L-Tyr-OBzl 在 chiral stationary phase including isopropyl-functionalized CF₆ 作用下， 以 乙醇 、 正庚烷 、 三氟乙酸 为溶剂， 生成 L-tyrosine benzyl ester 、 D-酪氨酸苄酯
  参考文献：
  名称：

  [EN] COMPOSITIONS AND METHODS FOR CYCLOFRUCTANS AS SEPARATION AGENTS
  [FR] COMPOSITIONS ET PROCÉDÉS POUR DES CYCLOFRUCTANES EN TANT QU'AGENTS DE SÉPARATION

  摘要：

  公开号：

  WO2010148191A3

文献信息

• NANNOCYSTIN PROCESS AND PRODUCTS
  申请人：THE RESEARCH FOUNDATION FOR THE STATE UNIVERSITY OF NEW YORK

  公开号：US20170320893A1

  公开（公告）日：2017-11-09

  Described herein is a process for the total synthesis of macrolactones and macrolactams of formula I including E- and Z-configuration thereof, in particular, nannocystins.

  本文描述了一种用于合成式I的大环内酯和大环内酰胺的全合成过程，包括其E-和Z-构型，特别是纳诺西斯汀。
• Total Syntheses of Nannocystins A and A0, Two Elongation Factor 1 Inhibitors
  作者：Jun Huang、Zhang Wang

  DOI：10.1021/acs.orglett.6b02352

  日期：2016.9.16

  Asymmetric total syntheses of nannocystins A and A0 were achieved in a convergent route starting from simple materials. Nannocystin family natural products bear potent anticancer activity as elongation factor 1 inhibitors. In this synthesis, the challenging tertiary amide bond was constructed by peptide coupling between an acyl chloride and a secondary amine. A late-stage ring-closing metathesis reaction

  从简单的材料开始，以收敛的方式实现了nannocystins A和A0的不对称总合成。Nannocystin系列天然产物具有作为延伸因子1抑制剂的有效抗癌活性。在该合成中，具有挑战性的叔酰胺键是通过酰氯和仲胺之间的肽偶联而构建的。晚期闭环复分解反应成功地产生了大环。这种有效的合成策略应适用于其他nannocystins和类似物，因此应有益于未来的结构-活性关系研究。
• Nannocystin process and products
  申请人：THE RESEARCH FOUNDATION FOR THE STATE UNIVERSITY OF NEW YORK

  公开号：US11230553B2

  公开（公告）日：2022-01-25

  Described herein is a process for the total synthesis of macrolactones and macrolactams of formula I including E- and Z-configuration thereof, in particular, nannocystins.

  本文描述的是式 I 的大内酯和大内酰胺的全合成工艺 包括其 E-和 Z-构型，特别是楠木内酯。
• Potent and selective 2-naphthylsulfonamide substituted hydroxamic acid inhibitors of matrix metalloproteinase-13
  作者：Ruben A. Tommasi、Sven Weiler、Leslie W. McQuire、Olivier Rogel、Mark Chambers、Kirk Clark、John Doughty、James Fang、Vishwas Ganu、Jonathan Grob、Ronald Goldberg、Robert Goldstein、Stacey LaVoie、Raviraj Kulathila、William Macchia、Richard Melton、Clayton Springer、Marc Walker、Jing Zhang、Lijuan Zhu、Michael Shultz

  DOI：10.1016/j.bmcl.2011.08.087

  日期：2011.11

  The matrix metalloproteinase enzyme MMP-13 plays a key role in the degradation of type II collagen in cartilage and bone in osteoarthritis (OA). An effective MMP-13 inhibitor would provide a disease modifying therapy for the treatment of arthritis, although this goal still continues to elude the pharmaceutical industry due to issues with safety. Our efforts have resulted in the discovery of a series of hydroxamic acid inhibitors of MMP-13 that do not significantly inhibit MMP-2 (gelatinase-1). MMP-2 has been implicated in the musculoskeletal side effects resulting from pan-MMP inhibition due to findings from spontaneously occurring human MMP-2 deletions. Analysis of the SAR of hundreds of previously prepared hydroxamate based MMP inhibitors lead us to 2-naphthylsulfonamide substituted hydroxamates which exhibited modest selectivity for MMP-13 versus MMP-2. This Letter describes the lead optimization of 1 and identification of inhibitors exhibiting >100-fold selectivity for MMP-13 over MMP-2 (C) 2011 Elsevier Ltd. All rights reserved.
• Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp
  作者：Jiro Arima、Hitomi Ito、Tadashi Hatanaka、Nobuhiro Mori

  DOI：10.1016/j.biochi.2011.04.020

  日期：2011.9

  From investigation of 2000 soil isolates, we identified two serine-type amidohydrolases that can hydrolyze D-aminoacyl derivatives from the culture supernatant of Streptomyces species 82F2 and 83D12. The enzymes, redesignated as 82F2-DAP and 83D12-DAP, were purified for homogeneity and characterized. Each enzyme had molecular mass of approximately 40 kDa, and each showed moderate stability with respect to temperature and pH. Among hydrolytic activities toward D-aminoacyl-pNAs, the enzymes showed strict specificity toward D-Phe-pNA, but showed broad specificity toward D-aminoacyl esters. The specific activity for D-Phe-pNA hydrolysis of 82F2-DAP was ten-fold higher than that of 83D12-DAP. As a second function, each enzyme showed peptide bond formation activity by its function of aminolysis reaction. Based on results of D-Phe D-Phe synthesis under various conditions, we propose a reaction mechanism for D-Phe D-Phe production. Furthermore, the enzymes exhibited peptide elongation activity, producing oligo homopeptide in a one-pot reaction. We cloned the genes encoding each enzyme, which revealed that the primary structure of each enzyme showed 30-60% identity with those of peptidases belonging to the clan SE, S12 peptidase family categorized as serine peptidase with D-stereospecificity. (C) 2011 Elsevier Masson SAS. All rights reserved.