(+)-tulipalin B | 95529-89-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: (+)-tulipalin B
• 英文别名: (+)-6-tulipalin B；R-(+)-tulipalin B；(4R)-4-hydroxy-3-methylideneoxolan-2-one
• CAS: 95529-89-8
• 化学式: C₅H₆O₃
• 分子量: 114.101
• InChiKey: BFLSLERVRLOFCX-BYPYZUCNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  8
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (+)-tulipalin B 在 1% Pd/C 、 氢气 作用下， 以 乙酸乙酯 为溶剂， 生成 (2R,3R)-3-hydroxy-2-methyl-butyrolactone 、 (2S,3R)-2-methyl-3-hydroxybutyrolactone
  参考文献：
  名称：

  The antibacterial properties of 6-tuliposide B. Synthesis of 6-tuliposide B analogues and structure–activity relationship

  摘要：

  6-Tuliposide B is a secondary metabolite occurring specifically in tulip anthers. Recently, a potent antibacterial activity of 6-tuliposide B has been reported. However, its molecular target has not yet been established, nor its action mechanism. To shed light on such issues, 6-tuliposide B and tulipalin B analogues were synthesized and a structure-activity relationship (SAR) was examined using a broad panel of bacterial strains. As the results of SAR among a total of 25 compounds, only tulipalin B and the compounds having 3',4'-dihydroxy-2'-methylenebutanoate (DHMB) moieties showed any significant antibacterial activity. Moreover, the 3'R analogues of these compounds displayed essentially the same activities as 6-tuliposide B and the structure of the 3'R-DMBA moiety was the same as that of the proposed active moiety of cnicin. These results suggest that 6-tuliposide B has the same action mechanism as proposed for cnicin and bacteria) MurA is one of the major molecular targets of 6-tuliposide B. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2009.10.008
• 作为产物：
  描述：

  epi-6-tuliposide B 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 24.0h， 以100%的产率得到(+)-tulipalin B
  参考文献：
  名称：

  First total synthesis of 6-tuliposide B

  摘要：

  Labile (+)-6-tuliposide B, an antimicrobial compound produced by tulip, was synthesized in nine steps from D-glucose via the Baylis-Hillman reaction of 2-(tert-butyldimethylsilyloxy)-acetaldehyde with 6-O-acryloyl-1-O-(2-trimethylsilylethyl)-beta-D-glucopyranoside, followed by a mild deprotection procedure using TFA in CH2Cl2. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2008.05.019

文献信息

• Molecular identification of tuliposide B-converting enzyme: a lactone-forming carboxylesterase from the pollen of tulip
  作者：Taiji Nomura、Tatsunori Murase、Shinjiro Ogita、Yasuo Kato

  DOI：10.1111/tpj.12883

  日期：2015.7

  Summary6‐Tuliposides A (PosA) and B (PosB), which are the major secondary metabolites in tulip (Tulipa gesneriana), are enzymatically converted to the antimicrobial lactonized aglycons, tulipalins A (PaA) and B (PaB), respectively. We recently identified a PosA‐converting enzyme (TCEA) as the first reported member of the lactone‐forming carboxylesterases. Herein, we describe the identification of another lactone‐forming carboxylesterase, PosB‐converting enzyme (TCEB), which preferentially reacts with PosB to give PaB. This enzyme was isolated from tulip pollen, which showed high PosB‐converting activity. Purified TCEB exhibited greater activity towards PosB than PosA, which was contrary to that of the TCEA. Novel cDNA (TgTCEB1) encoding the TCEB was isolated from tulip pollen. TgTCEB1 belonged to the carboxylesterase family and was approximately 50% identical to the TgTCEA polypeptides. Functional characterization of the recombinant enzyme verified that TgTCEB1 catalyzed the conversion of PosB to PaB with an activity comparable with the native TCEB. RT‐qPCR analysis of each part of plant revealed that TgTCEB1 transcripts were limited almost exclusively to the pollen. Furthermore, the immunostaining of the anther cross‐section using anti‐TgTCEB1 polyclonal antibody verified that TgTCEB1 was specifically expressed in the pollen grains, but not in the anther cells. N‐terminal transit peptide of TgTCEB1 was shown to function as plastid‐targeted signal. Taken together, these results indicate that mature TgTCEB1 is specifically localized in plastids of pollen grains. Interestingly, PosB, the substrate of TgTCEB1, accumulated on the pollen surface, but not in the intracellular spaces of pollen grains.
• First total synthesis of 6-tuliposide B
  作者：Kengo Shigetomi、Takao Kishimoto、Kazuaki Shoji、Makoto Ubukata

  DOI：10.1016/j.tetasy.2008.05.019

  日期：2008.6

  Labile (+)-6-tuliposide B, an antimicrobial compound produced by tulip, was synthesized in nine steps from D-glucose via the Baylis-Hillman reaction of 2-(tert-butyldimethylsilyloxy)-acetaldehyde with 6-O-acryloyl-1-O-(2-trimethylsilylethyl)-beta-D-glucopyranoside, followed by a mild deprotection procedure using TFA in CH2Cl2. (C) 2008 Elsevier Ltd. All rights reserved.
• The antibacterial properties of 6-tuliposide B. Synthesis of 6-tuliposide B analogues and structure–activity relationship
  作者：Kengo Shigetomi、Kazuaki Shoji、Shinya Mitsuhashi、Makoto Ubukata

  DOI：10.1016/j.phytochem.2009.10.008

  日期：2010.2

  6-Tuliposide B is a secondary metabolite occurring specifically in tulip anthers. Recently, a potent antibacterial activity of 6-tuliposide B has been reported. However, its molecular target has not yet been established, nor its action mechanism. To shed light on such issues, 6-tuliposide B and tulipalin B analogues were synthesized and a structure-activity relationship (SAR) was examined using a broad panel of bacterial strains. As the results of SAR among a total of 25 compounds, only tulipalin B and the compounds having 3',4'-dihydroxy-2'-methylenebutanoate (DHMB) moieties showed any significant antibacterial activity. Moreover, the 3'R analogues of these compounds displayed essentially the same activities as 6-tuliposide B and the structure of the 3'R-DMBA moiety was the same as that of the proposed active moiety of cnicin. These results suggest that 6-tuliposide B has the same action mechanism as proposed for cnicin and bacteria) MurA is one of the major molecular targets of 6-tuliposide B. (C) 2009 Elsevier Ltd. All rights reserved.