Chlorogenate anion

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: Chlorogenate anion
• 英文别名: (1S,3R,4R,5R)-3-[(E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy-1,4,5-trihydroxycyclohexane-1-carboxylate
• 化学式: C16H17O9-
• 分子量: 353.3
• InChiKey: CWVRJTMFETXNAD-JUHZACGLSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  25
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  168
• 氢给体数：
  5
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  Chlorogenate anion 、 D-saccharate 生成 2-O-Caffeoylglucarate 、 L-quinate
  参考文献：
  名称：

  Enzymic Synthesis of Caffeoylglucaric Acid from Chlorogenic Acid and Glucaric Acid by a Protein Preparation from Tomato Cotyledons

  摘要：

  对番茄（Lycopersicon esculentum Mill）子叶的苯丙烷代谢进行了研究。HPLC分析显示，两种羟基肉桂酸结合物为主要成分，分别为绿原酸（5-O-咖啡酰奎尼酸）和咖啡酰葡萄糖酸（2-O-或5-O-咖啡酰葡萄糖酸）。定量分析表明，绿原酸和咖啡酰葡萄糖酸之间存在前体-产物关系。研究发现，番茄子叶中的蛋白质制剂可催化咖啡酰葡萄糖酸的形成，其中绿原酸为酰基供体，游离葡萄糖酸为受体分子。这种酶活性可能属于羟基肉桂酰奎尼酸：葡萄糖酸羟基肉桂酰转移酶，与羟基肉桂酰-CoA：奎尼酸羟基肉桂酰转移酶共同作用。

  DOI：

  10.1104/pp.83.3.475

文献信息

• Isolation and Characterization of a Chlorogenic Acid Esterase from Aspergillus niger
  作者：B. Schöbel、W. Pollmann

  DOI：10.1515/znc-1980-3-407

  日期：1980.4.1

  The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The K_m-value is 0.70 mᴍ chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid.

  On the other hand a typical unspecific esterase like the pig liver esterases does not split chloro­genic acid.

  The isoelectric focusing reveals several isoenzymes of chlorogenase within a pI-range of 4.0-4.5.

  摘要 本文描述了一种特定的绿原酸酯酶的分离和表征。酶活性是通过测定水解产物咖啡酸来确定的。该酶已通过超滤和柱层析浓缩。pH和温度最适值分别为6.5和45°C。二价阳离子对酶活性不是必需的。与其他酯酶一样，这种酶被二异丙基氟磷酸酯抑制。Km值为0.70 mᴍ绿原酸，分子量为240000。所述酶对绿原酸具有特异性。 另一方面，像猪肝酯酶这样的典型非特异性酯酶无法分解绿原酸。 等电聚焦揭示了在pI范围为4.0-4.5内的几种绿原酸酶同工酶。
• Properties and Activity Changes of Chlorogenic Acid:Glucaric Acid Caffeoyltransferase From Tomato (<i>Lycopersicon esculentum</i>)
  作者：Dieter Strack、Wiltrud Gross

  DOI：10.1104/pp.92.1.41

  日期：1990.1.1

  A novel acyltransferase from cotyledons of tomato (Lycopersicon esculentum Mill.), which catalyzes the transfer of caffeic acid from chlorogenic acid (5-O-caffeoylquinic acid) to glucaric and galactaric acids, was purified with a 2400-fold enrichment and a 4% recovery. The enzyme showed specific activities (theoretical V  max per milligram of protein) of 625 nanokatals (caffeoylglucaric acid formation) and 310 nanokatals (caffeoylgalactaric acid formation). On sodium dodecyl sulfate-polyacrylamide gel electrophoresis it gave an apparent M  r of 40,000, identical to the value obtained by gel filtration column chromatography. Highest activity was found at pH 5.7, which was constant over a range of 20 to 120 millimolar K-phosphate. The isoelectric point of the enzyme was at pH 5.75. The reaction temperature optimum was at 38°C and the apparent energy of activation was calculated to be 57 kilojoules per mole. The apparent K  m values were 0.4 millimolar for glucaric acid, 1.7 millimolar for galactaric acid, and with both acceptors as second substrates 20 millimolar for chlorogenic acid. The relative ratio of the V  max/K  m values for glucaric acid and galactaric acid was found to be 100:12. Substrate-competition experiments support the conclusion that one single enzyme is responsible for both the glucaric and galactaric acid ester formation with marked preference for glucaric acid. It is proposed that the enzyme be called chlorogenic acid:glucaric acid O-caffeoyltransferase (EC 2.3.1.-). The three caffeic acid-dependent enzyme activities involved in the formation of the glucaric and galactaric acid esters, the chlorogenic acid:glucaric acid caffeoyltransferase as the key activity as well as the caffeic acid:CoA ligase and the caffeoyl-CoA:quinic acid caffeoyltransferase as the preceding activities, were determined. The time course of changes in these activities were followed during development of the seedling in the cotyledons and growth of the young plant in the first and second leaf. The results from tomato seedlings suggest a sequential appearance of these enzymes.

  oform（三氯甲烷）和氯仿（chloroform）是两种不同的有机溶剂，前者是易燃的，后者是易挥发的。
• Coffee pulp koji of Aspergillus sojae as stable immobilized catalyst of chlorogenate hydrolase
  作者：Osao Adachi、Yoshitaka Ano、Yoshihiko Akakabe、Emiko Shinagawa、Kazunobu Matsushita

  DOI：10.1007/s00253-008-1659-z

  日期：2008.11

  Chlorogenate hydrolase (EC 3.1.1.42, CHase) was highly induced in mycelia of Aspergillus sojae AKU 3312 grown in Czapek medium containing either instant coffee powder or coffee pulp as inducer. No CHase formation was observed in the mycelia when cultivated without the inducer. CHase was purified readily from CHase-induced mycelia to high homogeneity, and the purified CHase revealed the molecular weight of 180,000 consisting of two identical subunits of 88 kDa. Equimolar quinate (QA) and caffeate (CA) were confirmed on hydrolysis of chlorogenate (CGA). The purified CHase was only useful for a laboratory scale hydrolysis of CGA. For practical QA and CA production using scaled up hydrolysis of vegetable extracts of natural CGA resources, the enzyme activity of purified CHase decreased and denatured irreversibly. Preparation of coffee pulp koji and its application to QA and CA production were proposed instead of purified CHase. When coffee pulp koji was heated at 60 degrees C for 30 min, CHase survived without any appreciable loss of enzyme activity while vegetative mycelial growth and spore germination were terminated. The heated coffee pulp koji thus prepared was effective itself as stable immobilized catalyst of CHase for QA and CA production from vegetable CGA resources such as coffee powders, coffee pulp, and others.
• Schobel B.; Pollmann W., Z Naturforsch C Biosci, 1980, 0341-0382, 699-701
  作者：Schobel B.、Pollmann W.

  DOI：——

  日期：——