4-methylumbelliferone anion | 57980-13-9

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: 4-methylumbelliferone anion
• 英文别名: 4-Methyl-2-oxochromen-7-olate；4-methyl-2-oxochromen-7-olate
• CAS: 57980-13-9
• 化学式: C₁₀H₇O₃
• 分子量: 175.164
• InChiKey: HSHNITRMYYLLCV-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  13
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  49.4
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  4,6-O-Benzylidene-4-methylumbelliferyl-β-maltotriosyl-α-(1,6)-maltotrioside 在 β-glucosidase 、 α-glucosidase 、 pullulanase from Klebsiella planticola 作用下， 以 aq. acetate buffer 为溶剂， 生成 4-methylumbelliferone anion
  参考文献：
  名称：

  Colourimetric and fluorometric substrates for measurement of pullulanase activity

  摘要：

  Specific and highly sensitive colourimetric and fluorometric substrate mixtures have been prepared for the measurement of pullulanase and limit-dextrinase activity and assays employing these substrates have been developed. These mixtures comprise thermostable a-and b-glucosidases and either 4,6-Obenzylidene-2-chloro-4-nitrophenyl-b-maltotriosyl (1-6) a-maltotrioside (BzCNPG3G3, 1) as a colourimetric substrate or 4,6-O-benzylidene-4-methylumbelliferyl-b-maltotriosyl (1-6) a-maltotrioside (BzMUG3G3, 2) as a fluorometric substrate. Hydrolysis of substrates 1 and 2 by exo-acting enzymes such as amyloglucosidase, b-amylase and a-glucosidase is prevented by the presence of the 4,6-O-benzylidene group on the non-reducing end D-glucosyl residue. The substrates are not hydrolysed by any a-amylases studied, (including those from Aspergillus niger and porcine pancreas) and are resistant to hydrolysis by Pseudomonas sp. isoamylase. On hydrolysis by pullulanase, the 2-chloro-4-nitrophenyl-b-maltotrioside (3) or 4-methylumbelliferyl-b-maltotrioside (4) liberated is immediately hydrolysed to D-glucose and 2-chloro-4-nitrophenol or 4-methylumbelliferone. The reaction is terminated by the addition of a weak alkaline solution leading to the formation of phenolate ions in solution whose concentration can be determined using either spectrophotometric or fluorometric analysis. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2014.04.014

文献信息

• [EN] PHOSPHINATE ESTER-CONTAINING DYES HAVING TUNABLE PROPERTIES AND METHODS OF MAKING THE SAME<br/>[FR] COLORANTS CONTENANT UN ESTER DE PHOSPHINATE AYANT DES PROPRIÉTÉS POUVANT ÊTRE AJUSTÉES ET LEURS PROCÉDÉS DE FABRICATION
  申请人：UNIV VIRGINIA PATENT FOUNDATION

  公开号：WO2022241418A1

  公开（公告）日：2022-11-17

  In one aspect, the disclosure relates to xanthene-, thiazine-, and oxazine-based dyes containing a phosphinate ester group and having near-infrared (NIR) absorption and methods of making the same. The fluorescence lifetimes and stabilities of the dyes can be tuned by modifying the molecule cores, making them suitable for a variety of chemical labeling, imaging, and other theranostic applications. This abstract is intended as a scanning tool for purposes of searching in the particular art and is not intended to be limiting of the present disclosure.

  在某个方面，本公开涉及含有磷酸酯基团的黄酮类、噻唑类和噁唑类染料，具有近红外（NIR）吸收并制备方法。通过修改分子核心，可以调节染料的荧光寿命和稳定性，使其适用于各种化学标记、成像和其他治疗诊断应用。本摘要旨在作为搜索特定领域的扫描工具，不限制本公开内容。
• Chemoenzymatic synthesis of N-linked neoglycoproteins through a chitinase-catalyzed transglycosylation
  作者：Cishan Li、Wei Huang、Lai-Xi Wang

  DOI：10.1016/j.bmc.2008.08.042

  日期：2008.9

  A novel application of the Bacillus sp. chitinase for the chemoenzymatic synthesis of N-linked neoglycoproteins is described. Three chitinases with different molecular size were purified from the crude chitinase preparation. The purified chitinases were evaluated for their hydrolytic and transglycosylation activity. One chitinase with a molecular size of 100 kDa (Chi100) was identified to be the one with highest transglycosylation/ hydrolysis ratio. Chi100 could effectively recognize LacNAc-oxazoline and Man alpha 1,3Glc beta 1,4GlcNAc-oxazoline as the donor substrate to glycosylate Asn-linked GlcNAc, while it was unable to recognize Man beta 1,4GlcNAc and Man(3)GlcNAc-oxazolines as the donor substrates. The chitinase-catalyzed transglycosylation was successfully extended to the remodeling of ribonuclease B to afford neoglycoproteins. Although the yield needs to be optimized, the chitinase-catalyzed transglycosylation provides a potentially useful tool for the synthesis of neoglycoproteins carrying novel N-linked oligosaccharides. (C) 2008 Elsevier Ltd. All rights reserved.
• Colourimetric and fluorometric substrates for measurement of pullulanase activity
  作者：Barry V. McCleary、David Mangan、Vincent McKie、Claudio Cornaggia、Ruth Ivory、Edward Rooney

  DOI：10.1016/j.carres.2014.04.014

  日期：2014.7

  Specific and highly sensitive colourimetric and fluorometric substrate mixtures have been prepared for the measurement of pullulanase and limit-dextrinase activity and assays employing these substrates have been developed. These mixtures comprise thermostable a-and b-glucosidases and either 4,6-Obenzylidene-2-chloro-4-nitrophenyl-b-maltotriosyl (1-6) a-maltotrioside (BzCNPG3G3, 1) as a colourimetric substrate or 4,6-O-benzylidene-4-methylumbelliferyl-b-maltotriosyl (1-6) a-maltotrioside (BzMUG3G3, 2) as a fluorometric substrate. Hydrolysis of substrates 1 and 2 by exo-acting enzymes such as amyloglucosidase, b-amylase and a-glucosidase is prevented by the presence of the 4,6-O-benzylidene group on the non-reducing end D-glucosyl residue. The substrates are not hydrolysed by any a-amylases studied, (including those from Aspergillus niger and porcine pancreas) and are resistant to hydrolysis by Pseudomonas sp. isoamylase. On hydrolysis by pullulanase, the 2-chloro-4-nitrophenyl-b-maltotrioside (3) or 4-methylumbelliferyl-b-maltotrioside (4) liberated is immediately hydrolysed to D-glucose and 2-chloro-4-nitrophenol or 4-methylumbelliferone. The reaction is terminated by the addition of a weak alkaline solution leading to the formation of phenolate ions in solution whose concentration can be determined using either spectrophotometric or fluorometric analysis. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation. (C) 2014 Elsevier Ltd. All rights reserved.