(R)-Ketoprofenoyl-CoA | 430438-74-7

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: (R)-Ketoprofenoyl-CoA
• CAS: 430438-74-7
• 化学式: C₃₇H₄₈N₇O₁₈P₃S
• 分子量: 1003.81
• InChiKey: LSGSFYULVWAIJK-DEABNBTCSA-N

物化性质

• 密度：
  1.70±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  66.0
• 可旋转键数：
  23.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  380.7
• 氢给体数：
  9.0
• 氢受体数：
  20.0

反应信息

• 作为产物：
  描述：

  2-甲基-2-(3-苯甲酰基苯基)丙二酸 在 adenylate kinase 、 pyruvate kinase 、 磷烯醇丙酮酸 、 Mesorhizobium sp. BNC₁ arylmalonate decarboxylase 、 recombinant Luciola lateralis luciferase 、 5’-三磷酸腺苷 、 还原型辅酶Ⅰ 、 magnesium chloride 、 L-lactate dehydrogenase 作用下， 生成 (R)-Ketoprofenoyl-CoA
  参考文献：
  名称：

  Enantiodifferentiation of ketoprofen by Japanese firefly luciferase from Luciola lateralis

  摘要：

  Recently, we found that firefly luciferase exhibited (R)-enantioselective thioesterification activity toward 2-arylpropanoic acids. In the case of Japanese firefly luciferase from Luciola lateralis (LUG-H), the E-value for ketoprofen was approximately 20. In this study, we used a spectrophotometric method to measure the catalytic activity of LUG-H. Using this method allowed us to judge the reaction efficiency easily. Our results confirmed that LUG-H exhibits enantioselective thioesterification activity toward a series of 2-arylpropanoic acids. The highest activity was observed with ketoprofen. We also observed high enzymatic activity of LUC-H toward long-chain fatty acids. These results were reasonable because LUC-H is homologous with long-chain acyl-CoA synthetase. To obtain further information about the enantiodifferentiation mechanism of the LUC-H catalyzed thioesterification of ketoprofen, we determined the kinetic parameters of the reaction relative to each of its three substrates: ketoprofen, ATP, and coenzyme A (CoASH). We found that whereas the affinities of each compound are not affected by the chirality of ketoprofen, enantiodifferentiation is achieved by a chirality-dependent difference in the K(cat) parameter. (C) 2011 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2011.01.008

文献信息

• Comparison of Acyl-CoA Synthetic Activities and Enantioselectivity toward 2-Arylpropanoic Acids in Firefly Luciferases
  作者：Dai-ichiro KATO、Keisuke YOKOYAMA、Yoshihiro HIRAISHI、Masahiro TAKEO、Seiji NEGORO

  DOI：10.1271/bbb.110299

  日期：2011.9.23

  Measurement of thioesterification activities for dodecanoic acid (C12) and ketoprofen was done using five firefly luciferases, from Pyrocoelia miyako (PmL), Photinus pyralis (PpL), Luciola cruciata (LcL), Hotaria parvura (HpL), and Luciola mingrelica (LmL). Among these, PmL, PpL, and LcL showed the expected thioesterification activities toward both substrates. All the enzymes exhibited (R)-enantioselectivity toward ketoprofen, which had same tendency as firefly luciferase from Luciola lateralis (LUC-H). HpL and LmL, however, did not accept ketoprofen, although they had thioesterification activity toward C12. These results indicate that the substrate acceptance of luciferases for the thioesterification reaction varies dramatically relying on the origin of firefly. Hence we focused primarily on PmL and investigated the effect of pH on enzymatic activity. In addition, by determining the kinetic parameters at various pH values, we verified that the k  cat parameter contributed to the preferential enantioselectivity of this enzyme.

  使用五种萤火虫荧光素酶测定了十二酸（C12）和酮洛芬的硫酯化活性，这五种荧光素酶分别来自Pyrocoelia miyako（PmL）、Photinus pyralis（PpL）、Luciola cruciata（LcL）、Hotaria parvura（HpL）和Luciola mingrelica（LmL）。其中，PmL、PpL 和 LcL 对两种底物都表现出预期的硫酯化活性。所有酶都对酮洛芬表现出（R）-非对映选择性，这与来自Luciola lateralis的萤火虫荧光素酶（LUC-H）具有相同的倾向。然而，HpL 和 LmL 不接受酮洛芬，尽管它们对 C12 具有硫酯化活性。这些结果表明，硫酯化反应中荧光素酶对底物的接受程度因萤火虫来源的不同而有很大差异。因此，我们主要关注 PmL，并研究了 pH 值对酶活性的影响。此外，通过测定不同 pH 值下的动力学参数，我们验证了 k cat 参数有助于该酶的优先对映选择性。