3-(3,4-dioxo-cyclohexa-1,5-dienyl)-propionic acid | 2041-33-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3-(3,4-dioxo-cyclohexa-1,5-dienyl)-propionic acid
• 英文别名: 4-(2-Carboxy-ethyl)-benzochinon-(1,2) (o-Chinon d. Hydrokaffeesaeure)；3-(3,4-Dioxocyclohexa-1,5-dienyl)propanoic acid；3-(3,4-dioxocyclohexa-1,5-dien-1-yl)propanoic acid
• CAS: 2041-33-0
• 化学式: C₉H₈O₄
• 分子量: 180.16
• InChiKey: AEFCXEUJWYQCLS-UHFFFAOYSA-N

物化性质

• 熔点：
  105 °C (decomp)
• 沸点：
  389.0±34.0 °C(Predicted)
• 密度：
  1.357±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  13
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  71.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-(3,4-dioxo-cyclohexa-1,5-dienyl)-propionic acid 生成 3,4-二羟基苯基丙酸
  参考文献：
  名称：

  Enzymically Amplified Voltammetric Sensor for Microliter Sample Volumes of Salicylate

  摘要：

  A new voltammetric sensing strategy for salicylate employing two enzymes and applicable to microliter sample volumes is demonstrated, The method involves the use of the enzyme salicylate hydroxylase to convert salicylate to catechol, which is oxidized at a carbon electrode, The product of this oxidation reaction, o-quinone, is then reduced by a second enzyme, glucose oxidase, to regenerate catechol, Reoxidation of catechol results in a signal that is amplified due to repeated cycling of catechol molecules between the oxidized and reduced states, This chemistry is implemented in two configurations, (i) A paper disk into which both enzymes have been absorbed is mounted on a coplanar three electrode assembly for aqueous experiments, Determination of salicylate in a nonprescription dermatological product is demonstrated, (ii) A small solution volume confined directly on the coplanar electrodes is used for determination of salicylate in whole blood, The advantages of the use of two enzymes and of monitoring steady-state catalytic currents are discussed.

  DOI：

  10.1021/ac00107a022
• 作为产物：
  描述：

  3,4-二羟基苯基丙酸 在 polyphenol oxidase of Solanum melongena fruits 作用下， 生成 3-(3,4-dioxo-cyclohexa-1,5-dienyl)-propionic acid
  参考文献：
  名称：

  Use of Experimental Design Methodology To Prepare Maillard Reaction Products from Glucose and Cysteine Inhibitors of Polyphenol Oxidase from Eggplant (Solanum melongena)

  摘要：

  Polyphenol oxidase (PPO) from eggplant was extracted and partially purified by a two-step fractionation-precipitation using ammonium sulfate and phenylsepharose hydrophobic interaction chromatography. The eggplant PPO extract was characterized concerning its kinetic properties. Optimal conditions to obtain Maillard reaction products (MRPs) with a maximal inhibitory potency (IP) toward PPO activity were determined using the surface response methodology and a four-factor and five-level experimental design. The MRPs were prepared from cysteine (0.25 M) and glucose (0-1 M), at several initial pH values (2-6) and at differing heating times (3-19 h) and temperatures (95-115 degrees C). The maximal IP was obtained after heating a model system of glucose/cysteine (1/0.25 M) at pH 2 for 3 h 20 min at 115 degrees C. The soluble part of this MRP, called MRPIPmax, was a noncompetitive inhibitor toward eggplant PPO. The IP of MRPIPmax on PPO activity was very potent as compared to that displayed by benzoic, p-coumaric, and t-cinnamic acids, as well as sorbic acid and 4-hexylresorcinol. The activity of preincubated PPO at 0 degrees C with MRPIPmax was only slightly restored after dialysis or gel filtration.

  DOI：

  10.1021/jf060228r

文献信息

• Mechanistic Insight into the Activity of Tyrosinase from Variable-Temperature Studies in an Aqueous/Organic Solvent
  作者：Alessandro Granata、Enrico Monzani、Luigi Bubacco、Luigi Casella

  DOI：10.1002/chem.200501097

  日期：2006.3.8

  The activity of mushroom tyrosinase towards a representative series of phenolic and diphenolic substrates structurally related to tyrosine has been investigated in a mixed solvent of 34.4% methanol-glycerol (7:1, v/v) and 65.6% (v/v) aqueous 50 mM Hepes buffer at pH 6.8 at various temperatures. The kinetic activation parameters controlling the enzymatic reactions and the thermodynamic parameters associated

  在34.4％甲醇-甘油（7：1，v / v）和65.6％（v / v）50水溶液的混合溶剂中研究了蘑菇酪氨酸酶对与酪氨酸结构相关的代表性酚和二酚底物系列的活性在各种温度下，pH 6.8的mM Hepes缓冲液。已经从kcat和KM参数的温度变化推导了控制酶反应的动力学活化参数和与底物结合酶活性物质的过程相关的热力学参数。活化自由能由焓项主导，其值在61 +/- 9 kJ mol（-1）的相对狭窄范围内，而与底物或反应类型（单酚酶或双酚酶）无关。活化熵很小，通常为负，对活化自由能的贡献不超过10％。底物结合参数的特征在于焓和熵的贡献很大且为负，这通常由极性蛋白质与底物的相互作用所决定。底物4-羟苯基丙酸显示出惊人的温度依赖性的酶氧化速率，deltaH（双匕首）大约= 150 kJ mol（-1）和deltaS（double匕首）大约= 280 JK（-1）mol（- 1），因为它可以像其他底
• Omote, Yoshimori; Tomotake, Atsushi; Kashima, Choji, Journal of Chemical Research, Miniprint, 1987, # 1, p. 253 - 269
  作者：Omote, Yoshimori、Tomotake, Atsushi、Kashima, Choji

  DOI：——

  日期：——
• JEON, HEE-KYOUNG;NOHTA, HITOSHI;NAGAOKA, HIROAKI;OHKURA, YOSUKE, ANAL. SCI., 7,(1991) N, C. 257-262
  作者：JEON, HEE-KYOUNG、NOHTA, HITOSHI、NAGAOKA, HIROAKI、OHKURA, YOSUKE

  DOI：——

  日期：——
• OMOTE YOSHIMORI; TOMOTAKE ATSUSHI; KASHIMA CHOJI, J. CHEM. RES. SYNOP.,(1987) N 1, 10-11
  作者：OMOTE YOSHIMORI、 TOMOTAKE ATSUSHI、 KASHIMA CHOJI

  DOI：——

  日期：——